ATP-binding protein [Mixta gaviniae]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||||||
| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
542-789 | 1.30e-68 | |||||||||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; : Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 232.88 E-value: 1.30e-68
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| PRK09959 super family | cl32441 | acid-sensing system histidine kinase EvgS; |
74-997 | 2.78e-63 | |||||||||||||||
acid-sensing system histidine kinase EvgS; The actual alignment was detected with superfamily member PRK09959: Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 234.63 E-value: 2.78e-63
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| Name | Accession | Description | Interval | E-value | |||||||||||||||
| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
542-789 | 1.30e-68 | |||||||||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 232.88 E-value: 1.30e-68
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| PRK09959 | PRK09959 | acid-sensing system histidine kinase EvgS; |
74-997 | 2.78e-63 | |||||||||||||||
acid-sensing system histidine kinase EvgS; Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 234.63 E-value: 2.78e-63
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| PRK11091 | PRK11091 | aerobic respiration control sensor protein ArcB; Provisional |
563-926 | 1.74e-61 | |||||||||||||||
aerobic respiration control sensor protein ArcB; Provisional Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 224.82 E-value: 1.74e-61
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| TMAO_torS | TIGR02956 | TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ... |
564-1007 | 2.97e-60 | |||||||||||||||
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems] Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 223.89 E-value: 2.97e-60
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| PBP2_BvgS_D2 | cd13707 | The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
290-505 | 1.34e-45 | |||||||||||||||
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270425 [Multi-domain] Cd Length: 221 Bit Score: 163.54 E-value: 1.34e-45
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| HATPase_EvgS-ArcB-TorS-like | cd16922 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
684-788 | 2.13e-39 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 141.48 E-value: 2.13e-39
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| HATPase_c | smart00387 | Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
679-789 | 4.76e-36 | |||||||||||||||
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 132.00 E-value: 4.76e-36
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| HATPase_c | pfam02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
680-790 | 3.71e-32 | |||||||||||||||
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 120.94 E-value: 3.71e-32
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| HisJ | COG0834 | ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ... |
293-510 | 3.38e-30 | |||||||||||||||
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440596 [Multi-domain] Cd Length: 223 Bit Score: 119.31 E-value: 3.38e-30
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| BaeS_SmeS | NF012163 | sensor histidine kinase efflux regulator BaeS; |
565-787 | 1.36e-29 | |||||||||||||||
sensor histidine kinase efflux regulator BaeS; Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 123.40 E-value: 1.36e-29
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| SBP_bac_3 | pfam00497 | Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ... |
299-504 | 2.17e-24 | |||||||||||||||
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 425719 [Multi-domain] Cd Length: 221 Bit Score: 102.37 E-value: 2.17e-24
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| MtrAB_MtrB | NF040691 | MtrAB system histidine kinase MtrB; |
569-787 | 2.37e-18 | |||||||||||||||
MtrAB system histidine kinase MtrB; Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 89.70 E-value: 2.37e-18
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| PBPb | smart00062 | Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ... |
297-504 | 4.17e-16 | |||||||||||||||
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe Pssm-ID: 214497 [Multi-domain] Cd Length: 219 Bit Score: 78.52 E-value: 4.17e-16
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| AdeS_HK | NF012226 | two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ... |
576-788 | 4.89e-16 | |||||||||||||||
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline. Pssm-ID: 411090 [Multi-domain] Cd Length: 353 Bit Score: 80.81 E-value: 4.89e-16
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| Name | Accession | Description | Interval | E-value | |||||||||||||||
| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
542-789 | 1.30e-68 | |||||||||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 232.88 E-value: 1.30e-68
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| KdpD | COG2205 | K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
563-788 | 1.43e-68 | |||||||||||||||
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 229.41 E-value: 1.43e-68
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| WalK | COG5002 | Sensor histidine kinase WalK [Signal transduction mechanisms]; |
442-788 | 5.48e-65 | |||||||||||||||
Sensor histidine kinase WalK [Signal transduction mechanisms]; Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 224.82 E-value: 5.48e-65
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| PRK09959 | PRK09959 | acid-sensing system histidine kinase EvgS; |
74-997 | 2.78e-63 | |||||||||||||||
acid-sensing system histidine kinase EvgS; Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 234.63 E-value: 2.78e-63
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| PRK11091 | PRK11091 | aerobic respiration control sensor protein ArcB; Provisional |
563-926 | 1.74e-61 | |||||||||||||||
aerobic respiration control sensor protein ArcB; Provisional Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 224.82 E-value: 1.74e-61
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| TMAO_torS | TIGR02956 | TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ... |
564-1007 | 2.97e-60 | |||||||||||||||
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems] Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 223.89 E-value: 2.97e-60
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| PRK15347 | PRK15347 | two component system sensor kinase; |
563-991 | 1.23e-50 | |||||||||||||||
two component system sensor kinase; Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 193.70 E-value: 1.23e-50
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| PBP2_BvgS_D2 | cd13707 | The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
290-505 | 1.34e-45 | |||||||||||||||
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270425 [Multi-domain] Cd Length: 221 Bit Score: 163.54 E-value: 1.34e-45
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| COG4251 | COG4251 | Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
318-787 | 2.21e-43 | |||||||||||||||
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms]; Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 165.73 E-value: 2.21e-43
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| PRK11466 | PRK11466 | hybrid sensory histidine kinase TorS; Provisional |
564-875 | 2.22e-43 | |||||||||||||||
hybrid sensory histidine kinase TorS; Provisional Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 171.24 E-value: 2.22e-43
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| PRK10841 | PRK10841 | two-component system sensor histidine kinase RcsC; |
563-788 | 2.12e-40 | |||||||||||||||
two-component system sensor histidine kinase RcsC; Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 161.68 E-value: 2.12e-40
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| PBP2_BvgS_D1 | cd13705 | The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
50-265 | 4.76e-40 | |||||||||||||||
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270423 [Multi-domain] Cd Length: 221 Bit Score: 147.74 E-value: 4.76e-40
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| PRK11107 | PRK11107 | hybrid sensory histidine kinase BarA; Provisional |
564-936 | 7.16e-40 | |||||||||||||||
hybrid sensory histidine kinase BarA; Provisional Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 160.01 E-value: 7.16e-40
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| HATPase_EvgS-ArcB-TorS-like | cd16922 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
684-788 | 2.13e-39 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 141.48 E-value: 2.13e-39
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| COG4191 | COG4191 | Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
573-788 | 2.83e-38 | |||||||||||||||
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms]; Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 147.25 E-value: 2.83e-38
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| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
566-788 | 6.54e-37 | |||||||||||||||
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]; Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 144.72 E-value: 6.54e-37
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| HATPase_c | smart00387 | Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
679-789 | 4.76e-36 | |||||||||||||||
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 132.00 E-value: 4.76e-36
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| NtrB | COG3852 | Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
565-789 | 3.04e-34 | |||||||||||||||
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 135.36 E-value: 3.04e-34
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| PBP2_BvgS_HisK_like | cd01007 | The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ... |
290-504 | 3.79e-34 | |||||||||||||||
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270228 [Multi-domain] Cd Length: 220 Bit Score: 130.73 E-value: 3.79e-34
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| phoR_proteo | TIGR02966 | phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ... |
565-786 | 3.09e-32 | |||||||||||||||
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems] Pssm-ID: 274368 [Multi-domain] Cd Length: 333 Bit Score: 128.48 E-value: 3.09e-32
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| HATPase_c | pfam02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
680-790 | 3.71e-32 | |||||||||||||||
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. Pssm-ID: 460579 [Multi-domain] Cd Length: 109 Bit Score: 120.94 E-value: 3.71e-32
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| HisJ | COG0834 | ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ... |
293-510 | 3.38e-30 | |||||||||||||||
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440596 [Multi-domain] Cd Length: 223 Bit Score: 119.31 E-value: 3.38e-30
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| BaeS_SmeS | NF012163 | sensor histidine kinase efflux regulator BaeS; |
565-787 | 1.36e-29 | |||||||||||||||
sensor histidine kinase efflux regulator BaeS; Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 123.40 E-value: 1.36e-29
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| PRK10549 | PRK10549 | two-component system sensor histidine kinase BaeS; |
569-788 | 1.97e-27 | |||||||||||||||
two-component system sensor histidine kinase BaeS; Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 117.04 E-value: 1.97e-27
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| PRK11100 | PRK11100 | sensory histidine kinase CreC; Provisional |
580-789 | 2.01e-26 | |||||||||||||||
sensory histidine kinase CreC; Provisional Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 114.17 E-value: 2.01e-26
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| HATPase_BaeS-like | cd16946 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
680-787 | 3.71e-25 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain. Pssm-ID: 340422 [Multi-domain] Cd Length: 109 Bit Score: 101.00 E-value: 3.71e-25
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| PRK10604 | PRK10604 | sensor protein RstB; Provisional |
568-797 | 1.25e-24 | |||||||||||||||
sensor protein RstB; Provisional Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 108.15 E-value: 1.25e-24
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| KinE | COG5809 | Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
572-788 | 1.77e-24 | |||||||||||||||
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]; Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 108.52 E-value: 1.77e-24
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| SBP_bac_3 | pfam00497 | Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ... |
299-504 | 2.17e-24 | |||||||||||||||
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 425719 [Multi-domain] Cd Length: 221 Bit Score: 102.37 E-value: 2.17e-24
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| cztS_silS_copS | TIGR01386 | heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ... |
572-787 | 7.26e-23 | |||||||||||||||
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Pssm-ID: 273593 [Multi-domain] Cd Length: 457 Bit Score: 103.24 E-value: 7.26e-23
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| PRK11360 | PRK11360 | two-component system sensor histidine kinase AtoS; |
574-788 | 4.52e-22 | |||||||||||||||
two-component system sensor histidine kinase AtoS; Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 101.97 E-value: 4.52e-22
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| HATPase_AtoS-like | cd16943 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-788 | 4.96e-21 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains. Pssm-ID: 340419 [Multi-domain] Cd Length: 105 Bit Score: 89.02 E-value: 4.96e-21
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| PRK10490 | PRK10490 | sensor protein KdpD; Provisional |
563-796 | 9.31e-21 | |||||||||||||||
sensor protein KdpD; Provisional Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 98.57 E-value: 9.31e-21
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| PBP2_BvgS_HisK_like | cd01007 | The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ... |
50-264 | 1.99e-20 | |||||||||||||||
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270228 [Multi-domain] Cd Length: 220 Bit Score: 91.06 E-value: 1.99e-20
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| KinB | COG5806 | Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ... |
565-788 | 3.29e-20 | |||||||||||||||
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]; Pssm-ID: 444508 [Multi-domain] Cd Length: 412 Bit Score: 94.55 E-value: 3.29e-20
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| PRK09303 | PRK09303 | histidine kinase; |
569-787 | 1.67e-19 | |||||||||||||||
histidine kinase; Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 91.94 E-value: 1.67e-19
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| CitA | COG3290 | Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
564-788 | 3.33e-19 | |||||||||||||||
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms]; Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 91.06 E-value: 3.33e-19
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| PRK13837 | PRK13837 | two-component system VirA-like sensor kinase; |
575-861 | 6.43e-19 | |||||||||||||||
two-component system VirA-like sensor kinase; Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 92.43 E-value: 6.43e-19
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| HATPase_FilI-like | cd16921 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 8.14e-19 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340398 [Multi-domain] Cd Length: 105 Bit Score: 82.76 E-value: 8.14e-19
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| HATPase_YcbM-like | cd16947 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-786 | 9.89e-19 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA). Pssm-ID: 340423 [Multi-domain] Cd Length: 125 Bit Score: 83.33 E-value: 9.89e-19
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| MtrAB_MtrB | NF040691 | MtrAB system histidine kinase MtrB; |
569-787 | 2.37e-18 | |||||||||||||||
MtrAB system histidine kinase MtrB; Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 89.70 E-value: 2.37e-18
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| CheY | COG0784 | CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
806-924 | 3.88e-18 | |||||||||||||||
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms]; Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 81.44 E-value: 3.88e-18
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| HATPase_RstB-like | cd16939 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
690-788 | 5.62e-18 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain. Pssm-ID: 340416 [Multi-domain] Cd Length: 104 Bit Score: 80.17 E-value: 5.62e-18
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| HATPase_TutC-TodS-like | cd16925 | Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ... |
680-787 | 7.75e-18 | |||||||||||||||
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain. Pssm-ID: 340402 [Multi-domain] Cd Length: 110 Bit Score: 80.23 E-value: 7.75e-18
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| HATPase_BasS-like | cd16940 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-786 | 8.78e-18 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain. Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 80.14 E-value: 8.78e-18
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| PBP2_HisK | cd13704 | The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ... |
291-504 | 4.03e-17 | |||||||||||||||
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270422 [Multi-domain] Cd Length: 220 Bit Score: 81.48 E-value: 4.03e-17
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| REC_hyHK_CKI1_RcsC-like | cd17546 | phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ... |
812-924 | 4.95e-17 | |||||||||||||||
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381099 [Multi-domain] Cd Length: 113 Bit Score: 77.89 E-value: 4.95e-17
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| phoR | PRK11006 | phosphate regulon sensor histidine kinase PhoR; |
570-787 | 5.78e-17 | |||||||||||||||
phosphate regulon sensor histidine kinase PhoR; Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 84.68 E-value: 5.78e-17
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| KinA | COG5805 | Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
573-789 | 7.49e-17 | |||||||||||||||
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms]; Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 84.78 E-value: 7.49e-17
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| HATPase_CpxA-like | cd16949 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
690-788 | 1.47e-16 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain. Pssm-ID: 340425 [Multi-domain] Cd Length: 104 Bit Score: 76.21 E-value: 1.47e-16
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| PBP2_HisK_like_1 | cd13706 | Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This ... |
302-504 | 2.04e-16 | |||||||||||||||
Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This group includes periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270424 [Multi-domain] Cd Length: 219 Bit Score: 79.14 E-value: 2.04e-16
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| HATPase_TmoS-FixL-DctS-like | cd16920 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 2.60e-16 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340397 [Multi-domain] Cd Length: 104 Bit Score: 75.51 E-value: 2.60e-16
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| PBP2_peptides_like | cd13530 | Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ... |
299-504 | 2.88e-16 | |||||||||||||||
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 270248 [Multi-domain] Cd Length: 217 Bit Score: 78.83 E-value: 2.88e-16
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| HATPase_BceS-YxdK-YvcQ-like | cd16948 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
691-787 | 3.60e-16 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds. Pssm-ID: 340424 [Multi-domain] Cd Length: 109 Bit Score: 75.40 E-value: 3.60e-16
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| PBPb | smart00062 | Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ... |
297-504 | 4.17e-16 | |||||||||||||||
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe Pssm-ID: 214497 [Multi-domain] Cd Length: 219 Bit Score: 78.52 E-value: 4.17e-16
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| AdeS_HK | NF012226 | two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ... |
576-788 | 4.89e-16 | |||||||||||||||
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline. Pssm-ID: 411090 [Multi-domain] Cd Length: 353 Bit Score: 80.81 E-value: 4.89e-16
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| PleD | COG3706 | Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
809-972 | 5.82e-16 | |||||||||||||||
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription]; Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 76.87 E-value: 5.82e-16
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| PRK10618 | PRK10618 | phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional |
569-1007 | 5.98e-16 | |||||||||||||||
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 83.06 E-value: 5.98e-16
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| PRK09835 | PRK09835 | Cu(+)/Ag(+) sensor histidine kinase; |
571-787 | 8.53e-16 | |||||||||||||||
Cu(+)/Ag(+) sensor histidine kinase; Pssm-ID: 182101 [Multi-domain] Cd Length: 482 Bit Score: 81.36 E-value: 8.53e-16
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| PBP2_BvgS_D2 | cd13707 | The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
50-265 | 1.52e-15 | |||||||||||||||
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270425 [Multi-domain] Cd Length: 221 Bit Score: 76.87 E-value: 1.52e-15
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| RpfG | COG3437 | Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
808-925 | 1.70e-15 | |||||||||||||||
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms]; Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 76.74 E-value: 1.70e-15
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| HATPase_CreC-like | cd16945 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-786 | 5.80e-15 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS. Pssm-ID: 340421 [Multi-domain] Cd Length: 106 Bit Score: 71.72 E-value: 5.80e-15
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| PRK10364 | PRK10364 | two-component system sensor histidine kinase ZraS; |
576-790 | 7.61e-15 | |||||||||||||||
two-component system sensor histidine kinase ZraS; Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 78.29 E-value: 7.61e-15
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| HATPase_EnvZ-like | cd16950 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 8.27e-15 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain. Pssm-ID: 340426 [Multi-domain] Cd Length: 101 Bit Score: 70.94 E-value: 8.27e-15
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| HATPase_EcPhoR-like | cd16952 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 3.39e-14 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism. Pssm-ID: 340428 [Multi-domain] Cd Length: 108 Bit Score: 69.54 E-value: 3.39e-14
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| HATPase_PhoQ-like | cd16954 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
676-786 | 3.47e-14 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain. Pssm-ID: 340430 [Multi-domain] Cd Length: 135 Bit Score: 70.35 E-value: 3.47e-14
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| HisJ | COG0834 | ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ... |
52-252 | 4.80e-14 | |||||||||||||||
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440596 [Multi-domain] Cd Length: 223 Bit Score: 72.71 E-value: 4.80e-14
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| cpxA | PRK09470 | envelope stress sensor histidine kinase CpxA; |
568-788 | 1.26e-13 | |||||||||||||||
envelope stress sensor histidine kinase CpxA; Pssm-ID: 236532 [Multi-domain] Cd Length: 461 Bit Score: 74.58 E-value: 1.26e-13
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| HATPase_CckA-like | cd16919 | Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ... |
675-787 | 1.51e-13 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s). Pssm-ID: 340396 [Multi-domain] Cd Length: 116 Bit Score: 68.18 E-value: 1.51e-13
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| REC_RpfG-like | cd17551 | phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ... |
811-875 | 4.56e-13 | |||||||||||||||
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381103 [Multi-domain] Cd Length: 118 Bit Score: 66.70 E-value: 4.56e-13
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| envZ | PRK09467 | osmolarity sensor protein; Provisional |
669-789 | 5.18e-13 | |||||||||||||||
osmolarity sensor protein; Provisional Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 72.25 E-value: 5.18e-13
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| REC | cd00156 | phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
814-914 | 9.48e-13 | |||||||||||||||
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381085 [Multi-domain] Cd Length: 99 Bit Score: 65.33 E-value: 9.48e-13
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| ComP | COG4585 | Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
593-789 | 1.18e-12 | |||||||||||||||
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 68.88 E-value: 1.18e-12
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| Response_reg | pfam00072 | Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
812-924 | 1.30e-12 | |||||||||||||||
Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain. Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 65.25 E-value: 1.30e-12
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| HATPase_UhpB-NarQ-NarX-like | cd16917 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
686-787 | 2.13e-12 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains. Pssm-ID: 340394 [Multi-domain] Cd Length: 87 Bit Score: 63.73 E-value: 2.13e-12
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| HATPase_BvrS-ChvG-like | cd16953 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 2.84e-12 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain. Pssm-ID: 340429 [Multi-domain] Cd Length: 110 Bit Score: 64.13 E-value: 2.84e-12
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| PBP2_MidA_like | cd01004 | Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ... |
293-492 | 5.40e-12 | |||||||||||||||
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270225 [Multi-domain] Cd Length: 230 Bit Score: 66.50 E-value: 5.40e-12
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| OmpR | COG0745 | DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
809-924 | 5.86e-12 | |||||||||||||||
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription]; Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 66.13 E-value: 5.86e-12
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| nifL_nitrog | TIGR02938 | nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
565-788 | 6.59e-12 | |||||||||||||||
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions] Pssm-ID: 131984 [Multi-domain] Cd Length: 494 Bit Score: 69.16 E-value: 6.59e-12
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| HisKA | cd00082 | Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
568-628 | 6.77e-12 | |||||||||||||||
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes. Pssm-ID: 119399 [Multi-domain] Cd Length: 65 Bit Score: 61.46 E-value: 6.77e-12
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| HATPase_Glnl-NtrB-like | cd16918 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 6.85e-12 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s). Pssm-ID: 340395 [Multi-domain] Cd Length: 109 Bit Score: 63.19 E-value: 6.85e-12
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| PRK11086 | PRK11086 | sensory histidine kinase DcuS; Provisional |
690-787 | 1.40e-11 | |||||||||||||||
sensory histidine kinase DcuS; Provisional Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 68.40 E-value: 1.40e-11
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| HisKA | pfam00512 | His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
570-631 | 1.87e-11 | |||||||||||||||
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases. Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 60.30 E-value: 1.87e-11
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| HATPase_HupT_MifS-like | cd16976 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-786 | 1.90e-11 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain. Pssm-ID: 340435 [Multi-domain] Cd Length: 102 Bit Score: 61.70 E-value: 1.90e-11
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| marine_sort_HK | TIGR03785 | proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ... |
574-787 | 3.03e-11 | |||||||||||||||
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase. Pssm-ID: 163497 [Multi-domain] Cd Length: 703 Bit Score: 67.46 E-value: 3.03e-11
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| PRK13557 | PRK13557 | histidine kinase; Provisional |
716-873 | 4.21e-11 | |||||||||||||||
histidine kinase; Provisional Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 66.62 E-value: 4.21e-11
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| HisKA | smart00388 | His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
570-631 | 4.46e-11 | |||||||||||||||
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases. Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 59.12 E-value: 4.46e-11
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| REC | smart00448 | cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ... |
810-864 | 7.07e-11 | |||||||||||||||
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues. Pssm-ID: 214668 [Multi-domain] Cd Length: 55 Bit Score: 58.35 E-value: 7.07e-11
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| HATPase_NtrY-like | cd16944 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
680-787 | 8.71e-11 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains. Pssm-ID: 340420 [Multi-domain] Cd Length: 108 Bit Score: 59.86 E-value: 8.71e-11
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| SBP_bac_3 | pfam00497 | Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ... |
52-264 | 1.27e-10 | |||||||||||||||
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 425719 [Multi-domain] Cd Length: 221 Bit Score: 62.31 E-value: 1.27e-10
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| HATPase_VanS-like | cd16923 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-785 | 1.53e-10 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain. Pssm-ID: 340400 [Multi-domain] Cd Length: 102 Bit Score: 58.94 E-value: 1.53e-10
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| HATPase_DpiB-CitA-like | cd16915 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
687-787 | 1.90e-10 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain. Pssm-ID: 340392 [Multi-domain] Cd Length: 104 Bit Score: 58.84 E-value: 1.90e-10
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| PBP2_BvgS_D1 | cd13705 | The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
290-505 | 2.03e-10 | |||||||||||||||
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270423 [Multi-domain] Cd Length: 221 Bit Score: 61.84 E-value: 2.03e-10
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| AtoC | COG2204 | DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
808-998 | 2.57e-10 | |||||||||||||||
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms]; Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 63.83 E-value: 2.57e-10
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| HPtr | COG2198 | HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
186-1007 | 3.81e-10 | |||||||||||||||
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 64.30 E-value: 3.81e-10
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| PRK10337 | PRK10337 | sensor protein QseC; Provisional |
565-785 | 4.25e-10 | |||||||||||||||
sensor protein QseC; Provisional Pssm-ID: 182388 [Multi-domain] Cd Length: 449 Bit Score: 63.13 E-value: 4.25e-10
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| PBP2_Cys_DEBP_like | cd01000 | Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ... |
292-472 | 8.51e-10 | |||||||||||||||
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270221 [Multi-domain] Cd Length: 228 Bit Score: 60.01 E-value: 8.51e-10
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| COG4192 | COG4192 | Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
671-787 | 1.28e-09 | |||||||||||||||
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms]; Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 62.01 E-value: 1.28e-09
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| YesM | COG2972 | Sensor histidine kinase YesM [Signal transduction mechanisms]; |
672-788 | 2.29e-09 | |||||||||||||||
Sensor histidine kinase YesM [Signal transduction mechanisms]; Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 60.80 E-value: 2.29e-09
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| REC_PA4781-like | cd19920 | phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ... |
814-875 | 3.87e-09 | |||||||||||||||
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381147 [Multi-domain] Cd Length: 103 Bit Score: 54.82 E-value: 3.87e-09
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| PBP2_GltI_DEBP | cd13688 | Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ... |
300-487 | 4.99e-09 | |||||||||||||||
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold; This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270406 [Multi-domain] Cd Length: 238 Bit Score: 58.03 E-value: 4.99e-09
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| COG3920 | COG3920 | Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
687-789 | 5.76e-09 | |||||||||||||||
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms]; Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 59.92 E-value: 5.76e-09
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| RsbW | COG2172 | Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
687-788 | 6.90e-09 | |||||||||||||||
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 54.92 E-value: 6.90e-09
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| AmiR | COG3707 | Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
808-972 | 9.81e-09 | |||||||||||||||
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 56.12 E-value: 9.81e-09
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| REC_D1_PleD-like | cd17538 | first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ... |
811-875 | 1.14e-08 | |||||||||||||||
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381093 [Multi-domain] Cd Length: 104 Bit Score: 53.66 E-value: 1.14e-08
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| REC_2_DhkD-like | cd17580 | second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ... |
812-873 | 1.23e-08 | |||||||||||||||
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 54.00 E-value: 1.23e-08
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| CitB | COG4565 | DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
807-925 | 1.75e-08 | |||||||||||||||
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms]; Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 54.21 E-value: 1.75e-08
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| PBP2_GluR0 | cd00997 | Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ... |
291-439 | 3.06e-08 | |||||||||||||||
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. The GluR0 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270218 [Multi-domain] Cd Length: 218 Bit Score: 55.42 E-value: 3.06e-08
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| HATPase_PDK-like | cd16929 | Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ... |
704-787 | 4.17e-08 | |||||||||||||||
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids. Pssm-ID: 340406 [Multi-domain] Cd Length: 169 Bit Score: 53.88 E-value: 4.17e-08
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| PBP2_BvgS_like_1 | cd13708 | Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ... |
393-504 | 4.23e-08 | |||||||||||||||
Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270426 [Multi-domain] Cd Length: 220 Bit Score: 54.82 E-value: 4.23e-08
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| YesN | COG4753 | Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ... |
811-914 | 4.42e-08 | |||||||||||||||
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 443786 [Multi-domain] Cd Length: 103 Bit Score: 52.08 E-value: 4.42e-08
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| PBP2_Atu4678_like | cd13696 | The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ... |
303-474 | 5.05e-08 | |||||||||||||||
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270414 [Multi-domain] Cd Length: 227 Bit Score: 54.69 E-value: 5.05e-08
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| UhpB | COG3851 | Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ... |
545-796 | 1.14e-07 | |||||||||||||||
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms]; Pssm-ID: 443060 [Multi-domain] Cd Length: 493 Bit Score: 55.78 E-value: 1.14e-07
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| PBP2_peptides_like | cd13530 | Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ... |
51-252 | 1.22e-07 | |||||||||||||||
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 270248 [Multi-domain] Cd Length: 217 Bit Score: 53.41 E-value: 1.22e-07
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| PBP2_SMa0082_like | cd01072 | The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ... |
298-484 | 1.33e-07 | |||||||||||||||
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Sinorhizobium meliloti and its related proteins. The putative SMa0082-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270233 [Multi-domain] Cd Length: 238 Bit Score: 53.81 E-value: 1.33e-07
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| LytT | COG3279 | DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ... |
809-924 | 2.10e-07 | |||||||||||||||
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms]; Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 52.90 E-value: 2.10e-07
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| PBP2_HisJ_LAO | cd13703 | Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; ... |
303-502 | 3.36e-07 | |||||||||||||||
Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; the type 2 periplasmic-binding protein fold; This subgroup includes the periplasmic-binding proteins, HisJ and LAO, that serve as initial receptors in the ABC transport of histidine and lysine-arginine-ornithine amino acids. They are belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270421 [Multi-domain] Cd Length: 229 Bit Score: 52.25 E-value: 3.36e-07
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| PBP2_HisJ_LAO_like | cd01001 | Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ... |
303-492 | 3.63e-07 | |||||||||||||||
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and related proteins; the type 2 periplasmic-binding protein fold; This family comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270222 [Multi-domain] Cd Length: 228 Bit Score: 52.30 E-value: 3.63e-07
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| PBP2_Cystine_like_1 | cd13713 | Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ... |
297-495 | 4.77e-07 | |||||||||||||||
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270431 [Multi-domain] Cd Length: 218 Bit Score: 51.90 E-value: 4.77e-07
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| PBP2_GlnP | cd13619 | Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ... |
303-440 | 1.27e-06 | |||||||||||||||
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily; Periplasmic glutamine binding domain GlnP serves as an initial receptor in the ABC transport of glutamine in eubacteria. GlnP belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270337 [Multi-domain] Cd Length: 220 Bit Score: 50.39 E-value: 1.27e-06
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| HATPase_SpaK_NisK-like | cd16975 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
680-784 | 1.31e-06 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals. Pssm-ID: 340434 [Multi-domain] Cd Length: 107 Bit Score: 47.84 E-value: 1.31e-06
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| HATPase_ETR2_ERS2-EIN4-like | cd16938 | Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ... |
673-786 | 1.37e-06 | |||||||||||||||
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340415 [Multi-domain] Cd Length: 133 Bit Score: 48.61 E-value: 1.37e-06
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| CitB | COG2197 | DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ... |
809-875 | 1.76e-06 | |||||||||||||||
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 441799 [Multi-domain] Cd Length: 131 Bit Score: 48.35 E-value: 1.76e-06
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| HATPase_YpdA-YehU-LytS-like | cd16924 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 2.96e-06 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain. Pssm-ID: 340401 [Multi-domain] Cd Length: 103 Bit Score: 46.67 E-value: 2.96e-06
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| REC_NarL-like | cd17535 | phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ... |
812-875 | 4.52e-06 | |||||||||||||||
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381090 [Multi-domain] Cd Length: 117 Bit Score: 46.74 E-value: 4.52e-06
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| PRK11644 | PRK11644 | signal transduction histidine-protein kinase/phosphatase UhpB; |
683-788 | 5.06e-06 | |||||||||||||||
signal transduction histidine-protein kinase/phosphatase UhpB; Pssm-ID: 236945 [Multi-domain] Cd Length: 495 Bit Score: 50.36 E-value: 5.06e-06
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| MltF | COG4623 | Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ... |
297-496 | 5.61e-06 | |||||||||||||||
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms]; Pssm-ID: 443662 [Multi-domain] Cd Length: 421 Bit Score: 50.06 E-value: 5.61e-06
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| REC_OmpR_PrrA-like | cd17627 | phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ... |
812-875 | 6.31e-06 | |||||||||||||||
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381142 [Multi-domain] Cd Length: 116 Bit Score: 46.22 E-value: 6.31e-06
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| PBP2_BsGlnH | cd13689 | Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ... |
293-504 | 7.66e-06 | |||||||||||||||
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold; This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270407 [Multi-domain] Cd Length: 229 Bit Score: 48.38 E-value: 7.66e-06
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| HATPase_Phy-like | cd16932 | Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ... |
680-771 | 1.13e-05 | |||||||||||||||
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events. Pssm-ID: 340409 [Multi-domain] Cd Length: 113 Bit Score: 45.34 E-value: 1.13e-05
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| PBP2_Arg_Lys_His | cd13624 | Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ... |
299-492 | 1.21e-05 | |||||||||||||||
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ArtJ of the ATP-binding cassette (ABC) transport system from the thermophilic bacterium Geobacillus stearothermophilus, which is specific for arginine, lysine, and histidine. ArtJ belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270342 [Multi-domain] Cd Length: 219 Bit Score: 47.49 E-value: 1.21e-05
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| REC_DivK-like | cd17548 | phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ... |
811-875 | 1.30e-05 | |||||||||||||||
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381100 [Multi-domain] Cd Length: 115 Bit Score: 45.22 E-value: 1.30e-05
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| PBP2_FliY | cd13712 | Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ... |
297-504 | 1.42e-05 | |||||||||||||||
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic binding protein fold; This group contains cystine binding domain FliY and its related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270430 [Multi-domain] Cd Length: 219 Bit Score: 47.38 E-value: 1.42e-05
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| REC_CheY4-like | cd17562 | phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ... |
811-875 | 6.53e-05 | |||||||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381110 [Multi-domain] Cd Length: 118 Bit Score: 43.44 E-value: 6.53e-05
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| HATPase_RsbW-like | cd16936 | Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ... |
691-786 | 1.00e-04 | |||||||||||||||
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B. Pssm-ID: 340413 [Multi-domain] Cd Length: 91 Bit Score: 42.26 E-value: 1.00e-04
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| REC_TPR | cd17589 | phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ... |
814-863 | 1.25e-04 | |||||||||||||||
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues. Pssm-ID: 381123 [Multi-domain] Cd Length: 115 Bit Score: 42.63 E-value: 1.25e-04
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| PRK10935 | PRK10935 | nitrate/nitrite two-component system sensor histidine kinase NarQ; |
694-793 | 1.46e-04 | |||||||||||||||
nitrate/nitrite two-component system sensor histidine kinase NarQ; Pssm-ID: 236800 [Multi-domain] Cd Length: 565 Bit Score: 45.61 E-value: 1.46e-04
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| PBP2_Ehub_like | cd01002 | Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 ... |
303-452 | 1.53e-04 | |||||||||||||||
Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 periplasmic binding protein fold; This family represents the periplasmic substrate-binding component of ABC transport systems that involved in uptake of osmoprotectants (also termed compatible solutes) such as ectoine and hydroxyectoine. To counteract the efflux of water, bacteria and archaea accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270223 [Multi-domain] Cd Length: 242 Bit Score: 44.58 E-value: 1.53e-04
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| REC_OmpR_MtPhoP-like | cd17615 | phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ... |
811-875 | 1.63e-04 | |||||||||||||||
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381131 [Multi-domain] Cd Length: 118 Bit Score: 42.34 E-value: 1.63e-04
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| REC_CheY_CheY3 | cd19923 | phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ... |
810-899 | 1.65e-04 | |||||||||||||||
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381150 [Multi-domain] Cd Length: 119 Bit Score: 42.33 E-value: 1.65e-04
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| Hpt | pfam01627 | Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ... |
954-1007 | 1.79e-04 | |||||||||||||||
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072). Pssm-ID: 426352 [Multi-domain] Cd Length: 84 Bit Score: 41.18 E-value: 1.79e-04
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| REC_OmpR | cd17574 | phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ... |
814-875 | 2.02e-04 | |||||||||||||||
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381116 [Multi-domain] Cd Length: 99 Bit Score: 41.24 E-value: 2.02e-04
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| PRK10755 | PRK10755 | two-component system sensor histidine kinase PmrB; |
573-787 | 2.40e-04 | |||||||||||||||
two-component system sensor histidine kinase PmrB; Pssm-ID: 236751 [Multi-domain] Cd Length: 356 Bit Score: 44.57 E-value: 2.40e-04
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| CheA | COG0643 | Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
743-791 | 2.47e-04 | |||||||||||||||
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 44.79 E-value: 2.47e-04
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| glnL | PRK11073 | nitrogen regulation protein NR(II); |
678-788 | 2.96e-04 | |||||||||||||||
nitrogen regulation protein NR(II); Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 44.30 E-value: 2.96e-04
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| PBP2_Arg_STM4351 | cd13700 | Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding ... |
292-504 | 3.33e-04 | |||||||||||||||
Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding protein fold; This group includes domains similar to Escherichia coli arginine third transport system. STM4351 is the high arginine specific periplasmic-binding protein of ABC transport system. STM4351 belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270418 [Multi-domain] Cd Length: 222 Bit Score: 43.20 E-value: 3.33e-04
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| REC_typeB_ARR-like | cd17584 | phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ... |
812-868 | 4.17e-04 | |||||||||||||||
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381121 [Multi-domain] Cd Length: 115 Bit Score: 41.07 E-value: 4.17e-04
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| PRK10600 | PRK10600 | nitrate/nitrite two-component system sensor histidine kinase NarX; |
684-799 | 4.25e-04 | |||||||||||||||
nitrate/nitrite two-component system sensor histidine kinase NarX; Pssm-ID: 182581 [Multi-domain] Cd Length: 569 Bit Score: 44.28 E-value: 4.25e-04
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| PRK10815 | PRK10815 | two-component system sensor histidine kinase PhoQ; |
690-782 | 4.56e-04 | |||||||||||||||
two-component system sensor histidine kinase PhoQ; Pssm-ID: 182754 [Multi-domain] Cd Length: 485 Bit Score: 43.85 E-value: 4.56e-04
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| REC_ETR-like | cd19933 | phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ... |
810-924 | 5.27e-04 | |||||||||||||||
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381160 [Multi-domain] Cd Length: 117 Bit Score: 40.85 E-value: 5.27e-04
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| PBP2_AA_binding_like_1 | cd13625 | Substrate-binding domain of putative amino acid-binding protein; the type 2 ... |
303-489 | 9.35e-04 | |||||||||||||||
Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold; This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270343 [Multi-domain] Cd Length: 230 Bit Score: 41.98 E-value: 9.35e-04
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| HATPase_EL346-LOV-HK-like | cd16951 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
684-787 | 1.14e-03 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain. Pssm-ID: 340427 [Multi-domain] Cd Length: 131 Bit Score: 40.09 E-value: 1.14e-03
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| HATPase_RsbT-like | cd16934 | Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ... |
678-783 | 1.21e-03 | |||||||||||||||
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B. Pssm-ID: 340411 [Multi-domain] Cd Length: 117 Bit Score: 39.66 E-value: 1.21e-03
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| HATPase_YehU-like | cd16956 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
691-787 | 1.22e-03 | |||||||||||||||
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain. Pssm-ID: 340432 [Multi-domain] Cd Length: 101 Bit Score: 39.34 E-value: 1.22e-03
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| REC_RocR | cd17530 | phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ... |
810-873 | 2.52e-03 | |||||||||||||||
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381086 [Multi-domain] Cd Length: 123 Bit Score: 38.96 E-value: 2.52e-03
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| REC_CpdR_CckA-like | cd18160 | phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ... |
811-875 | 2.80e-03 | |||||||||||||||
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381144 [Multi-domain] Cd Length: 103 Bit Score: 38.25 E-value: 2.80e-03
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| COG4567 | COG4567 | DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ... |
811-941 | 3.23e-03 | |||||||||||||||
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 443624 [Multi-domain] Cd Length: 177 Bit Score: 39.51 E-value: 3.23e-03
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| REC_OmpR_BsPhoP-like | cd19937 | phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ... |
814-875 | 3.27e-03 | |||||||||||||||
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381164 [Multi-domain] Cd Length: 116 Bit Score: 38.41 E-value: 3.27e-03
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| HATPase_c_2 | pfam13581 | Histidine kinase-like ATPase domain; |
668-785 | 3.35e-03 | |||||||||||||||
Histidine kinase-like ATPase domain; Pssm-ID: 433327 [Multi-domain] Cd Length: 127 Bit Score: 38.81 E-value: 3.35e-03
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| FixJ | COG4566 | DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ... |
812-875 | 4.20e-03 | |||||||||||||||
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription]; Pssm-ID: 443623 [Multi-domain] Cd Length: 196 Bit Score: 39.70 E-value: 4.20e-03
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| REC_PatA-like | cd17602 | phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ... |
812-875 | 4.47e-03 | |||||||||||||||
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues. Pssm-ID: 381129 [Multi-domain] Cd Length: 102 Bit Score: 37.73 E-value: 4.47e-03
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| REC_DctD-like | cd17549 | phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ... |
812-868 | 4.97e-03 | |||||||||||||||
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Pssm-ID: 381101 [Multi-domain] Cd Length: 130 Bit Score: 38.24 E-value: 4.97e-03
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| dpiB | PRK15053 | sensor histidine kinase DpiB; Provisional |
679-787 | 5.29e-03 | |||||||||||||||
sensor histidine kinase DpiB; Provisional Pssm-ID: 185013 [Multi-domain] Cd Length: 545 Bit Score: 40.59 E-value: 5.29e-03
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| PRK10610 | PRK10610 | chemotaxis protein CheY; |
810-868 | 6.53e-03 | |||||||||||||||
chemotaxis protein CheY; Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 38.03 E-value: 6.53e-03
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| HATPase_SpoIIAB-like | cd16942 | Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ... |
689-785 | 8.06e-03 | |||||||||||||||
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F. Pssm-ID: 340418 [Multi-domain] Cd Length: 135 Bit Score: 37.90 E-value: 8.06e-03
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