MULTISPECIES: PAS domain S-box protein [unclassified Pseudomonas]
Protein Classification
PBP2_BvgS_HisK_like and HATPase_UhpB-NarQ-NarX-like domain-containing protein; PBP2_BvgS_HisK_like and HATPase_UhpB-NarQ-NarX-like domain-containing protein; sensor histidine kinase; PBP2_BvgS_HisK_like and HATPase_UhpB-NarQ-NarX-like domain-containing protein; sensor histidine kinase; sensor histidine kinase; sensor histidine kinase( domain architecture ID 11541443)
protein containing domains PBP2_BvgS_HisK_like, PAS, and HATPase_UhpB-NarQ-NarX-like; protein containing domains PBP2_BvgS_HisK_like, PAS, and HATPase_UhpB-NarQ-NarX-like; sensor histidine kinase containing PAS and type 2 periplasmic-binding fold protein (PBP2) ligand-binding domains, functions as a protein kinase that phosphorylates target proteins in response to various signals; protein containing domains PBP2_BvgS_HisK_like, PAS, and HATPase_UhpB-NarQ-NarX-like; sensor histidine kinase containing PAS and type 2 periplasmic-binding fold protein (PBP2) ligand-binding domains, functions as a protein kinase that phosphorylates target proteins in response to various signals; sensor histidine kinase containing PAS and type 2 periplasmic-binding fold protein (PBP2) ligand-binding domains, functions as a protein kinase that phosphorylates target proteins in response to various signals; sensor histidine kinase containing PAS and type 2 periplasmic-binding fold protein (PBP2) ligand-binding domains, functions as a protein kinase that phosphorylates target proteins in response to various signals
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ComP | COG4585 | Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
569-787 | 4.33e-57 | |||||
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; : Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 195.61 E-value: 4.33e-57
|
|||||||||
| PBP2_BvgS_HisK_like | cd01007 | The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ... |
32-252 | 5.50e-46 | |||||
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: 163.86 E-value: 5.50e-46
|
|||||||||
| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
306-568 | 1.09e-24 | |||||
PAS domain [Signal transduction mechanisms]; : Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 103.95 E-value: 1.09e-24
|
|||||||||
| Name | Accession | Description | Interval | E-value | ||||||||
| ComP | COG4585 | Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
569-787 | 4.33e-57 | ||||||||
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 195.61 E-value: 4.33e-57
|
||||||||||||
| PBP2_BvgS_HisK_like | cd01007 | The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ... |
32-252 | 5.50e-46 | ||||||||
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: 163.86 E-value: 5.50e-46
|
||||||||||||
| HATPase_UhpB-NarQ-NarX-like | cd16917 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
698-782 | 2.16e-30 | ||||||||
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: 114.57 E-value: 2.16e-30
|
||||||||||||
| HisJ | COG0834 | ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ... |
35-257 | 4.77e-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: 118.54 E-value: 4.77e-30
|
||||||||||||
| PRK11644 | PRK11644 | signal transduction histidine-protein kinase/phosphatase UhpB; |
561-780 | 1.58e-29 | ||||||||
signal transduction histidine-protein kinase/phosphatase UhpB; Pssm-ID: 236945 [Multi-domain] Cd Length: 495 Bit Score: 123.16 E-value: 1.58e-29
|
||||||||||||
| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
306-568 | 1.09e-24 | ||||||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 103.95 E-value: 1.09e-24
|
||||||||||||
| PBPb | smart00062 | Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ... |
35-252 | 5.90e-22 | ||||||||
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe Pssm-ID: 214497 [Multi-domain] Cd Length: 219 Bit Score: 95.09 E-value: 5.90e-22
|
||||||||||||
| SBP_bac_3 | pfam00497 | Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ... |
35-252 | 2.30e-21 | ||||||||
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: 93.51 E-value: 2.30e-21
|
||||||||||||
| PRK13560 | PRK13560 | hypothetical protein; Provisional |
301-779 | 1.18e-16 | ||||||||
hypothetical protein; Provisional Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 84.72 E-value: 1.18e-16
|
||||||||||||
| HATPase_c | smart00387 | Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
693-782 | 4.06e-15 | ||||||||
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 71.91 E-value: 4.06e-15
|
||||||||||||
| HATPase_c | pfam02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
693-786 | 6.73e-15 | ||||||||
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: 71.25 E-value: 6.73e-15
|
||||||||||||
| PAS_3 | pfam08447 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
468-555 | 4.45e-11 | ||||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 59.66 E-value: 4.45e-11
|
||||||||||||
| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
312-436 | 5.82e-08 | ||||||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 51.91 E-value: 5.82e-08
|
||||||||||||
| PRK10859 | PRK10859 | membrane-bound lytic murein transglycosylase MltF; |
48-157 | 1.21e-07 | ||||||||
membrane-bound lytic murein transglycosylase MltF; Pssm-ID: 236778 [Multi-domain] Cd Length: 482 Bit Score: 54.88 E-value: 1.21e-07
|
||||||||||||
| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
335-426 | 8.56e-03 | ||||||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 36.46 E-value: 8.56e-03
|
||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||
| ComP | COG4585 | Signal transduction histidine kinase ComP [Signal transduction mechanisms]; |
569-787 | 4.33e-57 | ||||||||
Signal transduction histidine kinase ComP [Signal transduction mechanisms]; Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 195.61 E-value: 4.33e-57
|
||||||||||||
| PBP2_BvgS_HisK_like | cd01007 | The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ... |
32-252 | 5.50e-46 | ||||||||
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: 163.86 E-value: 5.50e-46
|
||||||||||||
| UhpB | COG3851 | Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ... |
557-781 | 3.18e-33 | ||||||||
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms]; Pssm-ID: 443060 [Multi-domain] Cd Length: 493 Bit Score: 134.36 E-value: 3.18e-33
|
||||||||||||
| HATPase_UhpB-NarQ-NarX-like | cd16917 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
698-782 | 2.16e-30 | ||||||||
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: 114.57 E-value: 2.16e-30
|
||||||||||||
| HisJ | COG0834 | ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ... |
35-257 | 4.77e-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: 118.54 E-value: 4.77e-30
|
||||||||||||
| PRK11644 | PRK11644 | signal transduction histidine-protein kinase/phosphatase UhpB; |
561-780 | 1.58e-29 | ||||||||
signal transduction histidine-protein kinase/phosphatase UhpB; Pssm-ID: 236945 [Multi-domain] Cd Length: 495 Bit Score: 123.16 E-value: 1.58e-29
|
||||||||||||
| PBP2_BvgS_D2 | cd13707 | The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
32-252 | 1.58e-25 | ||||||||
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: 105.38 E-value: 1.58e-25
|
||||||||||||
| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
306-568 | 1.09e-24 | ||||||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 103.95 E-value: 1.09e-24
|
||||||||||||
| PBPb | smart00062 | Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ... |
35-252 | 5.90e-22 | ||||||||
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe Pssm-ID: 214497 [Multi-domain] Cd Length: 219 Bit Score: 95.09 E-value: 5.90e-22
|
||||||||||||
| SBP_bac_3 | pfam00497 | Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ... |
35-252 | 2.30e-21 | ||||||||
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: 93.51 E-value: 2.30e-21
|
||||||||||||
| PBP2_HisK | cd13704 | The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ... |
43-252 | 3.32e-21 | ||||||||
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: 93.03 E-value: 3.32e-21
|
||||||||||||
| PBP2_BvgS_D1 | cd13705 | The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ... |
32-251 | 6.35e-21 | ||||||||
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: 91.89 E-value: 6.35e-21
|
||||||||||||
| PRK10600 | PRK10600 | nitrate/nitrite two-component system sensor histidine kinase NarX; |
588-781 | 2.04e-20 | ||||||||
nitrate/nitrite two-component system sensor histidine kinase NarX; Pssm-ID: 182581 [Multi-domain] Cd Length: 569 Bit Score: 95.89 E-value: 2.04e-20
|
||||||||||||
| PBP2_peptides_like | cd13530 | Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ... |
35-251 | 1.79e-19 | ||||||||
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: 87.69 E-value: 1.79e-19
|
||||||||||||
| KinA | COG5805 | Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
309-781 | 5.93e-18 | ||||||||
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: 87.86 E-value: 5.93e-18
|
||||||||||||
| PBP2_BvgS_like_1 | cd13708 | Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ... |
46-252 | 6.01e-17 | ||||||||
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: 80.63 E-value: 6.01e-17
|
||||||||||||
| PRK13560 | PRK13560 | hypothetical protein; Provisional |
301-779 | 1.18e-16 | ||||||||
hypothetical protein; Provisional Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 84.72 E-value: 1.18e-16
|
||||||||||||
| MltF | COG4623 | Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ... |
48-233 | 5.33e-16 | ||||||||
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms]; Pssm-ID: 443662 [Multi-domain] Cd Length: 421 Bit Score: 80.88 E-value: 5.33e-16
|
||||||||||||
| PRK10935 | PRK10935 | nitrate/nitrite two-component system sensor histidine kinase NarQ; |
588-781 | 8.14e-16 | ||||||||
nitrate/nitrite two-component system sensor histidine kinase NarQ; Pssm-ID: 236800 [Multi-domain] Cd Length: 565 Bit Score: 81.44 E-value: 8.14e-16
|
||||||||||||
| PBP2_YfhD_N | cd01009 | The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ... |
54-252 | 2.34e-15 | ||||||||
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They 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: 270230 [Multi-domain] Cd Length: 223 Bit Score: 76.10 E-value: 2.34e-15
|
||||||||||||
| HATPase_c | smart00387 | Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
693-782 | 4.06e-15 | ||||||||
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 71.91 E-value: 4.06e-15
|
||||||||||||
| HATPase_c | pfam02518 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
693-786 | 6.73e-15 | ||||||||
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: 71.25 E-value: 6.73e-15
|
||||||||||||
| NtrB | COG3852 | Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
312-450 | 4.39e-14 | ||||||||
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 74.50 E-value: 4.39e-14
|
||||||||||||
| KinE | COG5809 | Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
319-580 | 1.67e-12 | ||||||||
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: 70.39 E-value: 1.67e-12
|
||||||||||||
| KdpD | COG2205 | K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
567-782 | 2.91e-12 | ||||||||
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 67.24 E-value: 2.91e-12
|
||||||||||||
| PAS_3 | pfam08447 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
468-555 | 4.45e-11 | ||||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 59.66 E-value: 4.45e-11
|
||||||||||||
| PAS | COG2202 | PAS domain [Signal transduction mechanisms]; |
431-607 | 1.08e-10 | ||||||||
PAS domain [Signal transduction mechanisms]; Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 62.73 E-value: 1.08e-10
|
||||||||||||
| BaeS | COG0642 | Signal transduction histidine kinase [Signal transduction mechanisms]; |
486-781 | 1.89e-10 | ||||||||
Signal transduction histidine kinase [Signal transduction mechanisms]; Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 63.00 E-value: 1.89e-10
|
||||||||||||
| PBP2_HisK_like_1 | cd13706 | Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This ... |
44-252 | 1.91e-10 | ||||||||
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: 61.42 E-value: 1.91e-10
|
||||||||||||
| PBP2_HisJ_LAO_like | cd01001 | Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ... |
43-251 | 3.44e-10 | ||||||||
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: 60.77 E-value: 3.44e-10
|
||||||||||||
| HisKA_3 | pfam07730 | Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of ... |
589-656 | 3.62e-10 | ||||||||
Histidine kinase; This is the dimerization and phosphoacceptor domain of a sub-family of histidine kinases. It shares sequence similarity with pfam00512 and pfam07536. Pssm-ID: 429624 [Multi-domain] Cd Length: 68 Bit Score: 56.48 E-value: 3.62e-10
|
||||||||||||
| PBP2_HisJ_LAO | cd13703 | Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; ... |
35-251 | 7.54e-10 | ||||||||
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: 59.95 E-value: 7.54e-10
|
||||||||||||
| COG3920 | COG3920 | Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
288-786 | 3.16e-09 | ||||||||
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms]; Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 60.30 E-value: 3.16e-09
|
||||||||||||
| PAS_9 | pfam13426 | PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
335-428 | 7.17e-09 | ||||||||
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 53.62 E-value: 7.17e-09
|
||||||||||||
| PRK13560 | PRK13560 | hypothetical protein; Provisional |
414-585 | 3.99e-08 | ||||||||
hypothetical protein; Provisional Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 56.99 E-value: 3.99e-08
|
||||||||||||
| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
312-436 | 5.82e-08 | ||||||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 51.91 E-value: 5.82e-08
|
||||||||||||
| PRK10859 | PRK10859 | membrane-bound lytic murein transglycosylase MltF; |
48-157 | 1.21e-07 | ||||||||
membrane-bound lytic murein transglycosylase MltF; Pssm-ID: 236778 [Multi-domain] Cd Length: 482 Bit Score: 54.88 E-value: 1.21e-07
|
||||||||||||
| HATPase_EL346-LOV-HK-like | cd16951 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
693-782 | 1.24e-07 | ||||||||
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: 51.26 E-value: 1.24e-07
|
||||||||||||
| PAS_4 | pfam08448 | PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
322-431 | 1.96e-07 | ||||||||
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 50.11 E-value: 1.96e-07
|
||||||||||||
| COG4191 | COG4191 | Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
458-781 | 2.56e-07 | ||||||||
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms]; Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 53.65 E-value: 2.56e-07
|
||||||||||||
| KinE | COG5809 | Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
290-440 | 2.98e-07 | ||||||||
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: 53.83 E-value: 2.98e-07
|
||||||||||||
| PBP2_ArtJ | cd00999 | The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold ... |
44-209 | 3.36e-07 | ||||||||
The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold protein superfamily; An arginine-binding protein found in Chlamydiae trachomatis (CT-ArtJ) and pneumoniae (CPn-ArtJ) and its closely related proteins. CT- and CPn-ArtJ are shown to have different immunogenic properties despite a high sequence similarity. The ArtJ proteins display the type 2 periplasmic binding fold organized in two alpha-beta domains with arginine-binding region at their interface. Pssm-ID: 270220 [Multi-domain] Cd Length: 223 Bit Score: 51.94 E-value: 3.36e-07
|
||||||||||||
| PBP2_Cys_DEBP_like | cd01000 | Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ... |
35-233 | 3.47e-07 | ||||||||
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: 51.93 E-value: 3.47e-07
|
||||||||||||
| PRK11086 | PRK11086 | sensory histidine kinase DcuS; Provisional |
681-787 | 1.44e-06 | ||||||||
sensory histidine kinase DcuS; Provisional Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 51.84 E-value: 1.44e-06
|
||||||||||||
| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
292-438 | 1.59e-06 | ||||||||
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: 51.12 E-value: 1.59e-06
|
||||||||||||
| PBP2_Ala | cd13628 | Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ... |
44-172 | 2.27e-06 | ||||||||
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 periplasmic binding protein; This periplasmic substrate component serves as an initial receptor in the ABC transport of glutamine in eubacteria and archaea. After binding the alanine with high affinity, this domain Interacts 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. This alanine specific domain 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: 270346 [Multi-domain] Cd Length: 219 Bit Score: 49.39 E-value: 2.27e-06
|
||||||||||||
| RsbW | COG2172 | Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; |
701-784 | 2.36e-06 | ||||||||
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms]; Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 47.22 E-value: 2.36e-06
|
||||||||||||
| PBP2_FliY | cd13712 | Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ... |
35-251 | 2.42e-06 | ||||||||
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: 49.31 E-value: 2.42e-06
|
||||||||||||
| PBP2_PheC | cd01069 | Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ... |
43-118 | 2.55e-06 | ||||||||
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes cyclohexadienyl dehydratase PheC. These proteins catalyze the decarboxylation of prephenate to phenylpyruvate in the alternative phenylalanine biosynthesis pathway in some proteobacteria and archaea. The PheC proteins belong to the PBPII 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. Since they the PheC proteins are so similar to periplasmic binding proteins, (PBP), it is evolutionarily plausible that several pre-existing PBP proteins might have been recruited to perform the enzymatic function. Pssm-ID: 270231 [Multi-domain] Cd Length: 232 Bit Score: 49.26 E-value: 2.55e-06
|
||||||||||||
| PBP2_Cystine_like | cd13626 | Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ... |
43-233 | 2.59e-06 | ||||||||
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein fold; Cystine-binding domain of periplasmic receptor-dependent 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. Also, 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: 270344 [Multi-domain] Cd Length: 219 Bit Score: 49.24 E-value: 2.59e-06
|
||||||||||||
| HATPase_DpiB-CitA-like | cd16915 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
702-782 | 2.59e-06 | ||||||||
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: 46.51 E-value: 2.59e-06
|
||||||||||||
| COG4251 | COG4251 | Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
301-780 | 3.89e-06 | ||||||||
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms]; Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 50.17 E-value: 3.89e-06
|
||||||||||||
| PBP2_GlnH | cd00994 | Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ... |
57-251 | 4.18e-06 | ||||||||
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; This periplasmic substrate-binding component serves as an initial receptor in the ABC transport of glutamine in bacteria and eukaryota. GlnH 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: 270216 [Multi-domain] Cd Length: 218 Bit Score: 48.43 E-value: 4.18e-06
|
||||||||||||
| CitA | COG3290 | Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
572-787 | 5.85e-06 | ||||||||
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms]; Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 49.46 E-value: 5.85e-06
|
||||||||||||
| WalK | COG5002 | Sensor histidine kinase WalK [Signal transduction mechanisms]; |
483-787 | 7.03e-06 | ||||||||
Sensor histidine kinase WalK [Signal transduction mechanisms]; Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 49.17 E-value: 7.03e-06
|
||||||||||||
| PBP2_GlnP | cd13619 | Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ... |
43-116 | 1.64e-05 | ||||||||
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: 46.93 E-value: 1.64e-05
|
||||||||||||
| sensory_box | TIGR00229 | PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
439-568 | 2.45e-05 | ||||||||
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions] Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 44.20 E-value: 2.45e-05
|
||||||||||||
| HATPase_RsbW-like | cd16936 | Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ... |
701-740 | 4.03e-05 | ||||||||
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: 43.03 E-value: 4.03e-05
|
||||||||||||
| NtrY | COG5000 | Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
430-781 | 4.09e-05 | ||||||||
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: 46.88 E-value: 4.09e-05
|
||||||||||||
| PBP2_Atu4678_like | cd13696 | The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ... |
35-251 | 4.11e-05 | ||||||||
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: 45.83 E-value: 4.11e-05
|
||||||||||||
| HATPase_RstB-like | cd16939 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
698-750 | 5.99e-05 | ||||||||
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: 42.80 E-value: 5.99e-05
|
||||||||||||
| PBP2_GltS | cd13620 | Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ... |
43-117 | 8.85e-05 | ||||||||
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily; This family comprises of the periplasmic-binding protein component (GltS) of an ABC transporter specific for glutamate or arginine from Lactococcus lactis, as well as its closely related proteins. The GltS 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: 270338 [Multi-domain] Cd Length: 227 Bit Score: 44.64 E-value: 8.85e-05
|
||||||||||||
| PBP2_Arg_Lys_His | cd13624 | Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ... |
43-124 | 1.24e-04 | ||||||||
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: 44.02 E-value: 1.24e-04
|
||||||||||||
| PksD | COG3321 | Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
28-580 | 1.53e-04 | ||||||||
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 45.63 E-value: 1.53e-04
|
||||||||||||
| PBP2_AA_binding_like_3 | cd13621 | Substrate-binding domain of putative amino acid-binding protein; the type 2 ... |
35-117 | 1.68e-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: 270339 [Multi-domain] Cd Length: 229 Bit Score: 43.96 E-value: 1.68e-04
|
||||||||||||
| PRK13560 | PRK13560 | hypothetical protein; Provisional |
291-578 | 2.35e-04 | ||||||||
hypothetical protein; Provisional Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 44.66 E-value: 2.35e-04
|
||||||||||||
| CheA | COG0643 | Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; |
717-784 | 3.24e-04 | ||||||||
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms]; Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 44.02 E-value: 3.24e-04
|
||||||||||||
| PAS_8 | pfam13188 | PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
322-374 | 4.04e-04 | ||||||||
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 39.45 E-value: 4.04e-04
|
||||||||||||
| PRK13558 | PRK13558 | bacterio-opsin activator; Provisional |
311-518 | 4.51e-04 | ||||||||
bacterio-opsin activator; Provisional Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 43.67 E-value: 4.51e-04
|
||||||||||||
| PBP2_AA_hypothetical | cd13623 | Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic ... |
30-193 | 5.75e-04 | ||||||||
Substrate-binding domain of putative amino-acid transport system; 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: 270341 [Multi-domain] Cd Length: 220 Bit Score: 42.27 E-value: 5.75e-04
|
||||||||||||
| PBP2_Cystine_like_1 | cd13713 | Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ... |
54-252 | 9.78e-04 | ||||||||
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: 41.50 E-value: 9.78e-04
|
||||||||||||
| NtrB | COG3852 | Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
435-781 | 1.23e-03 | ||||||||
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 41.76 E-value: 1.23e-03
|
||||||||||||
| PBP2_Cysteine | cd13694 | Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ... |
35-193 | 1.25e-03 | ||||||||
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein fold; This subfamily comprises of the periplasmic-binding protein component of ABC transporter specific for cysteine and its closely related proteins. The cysteine-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: 270412 [Multi-domain] Cd Length: 229 Bit Score: 41.18 E-value: 1.25e-03
|
||||||||||||
| PBP2_MidA_like | cd01004 | Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ... |
35-114 | 1.74e-03 | ||||||||
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: 40.69 E-value: 1.74e-03
|
||||||||||||
| YesM | COG2972 | Sensor histidine kinase YesM [Signal transduction mechanisms]; |
670-787 | 2.00e-03 | ||||||||
Sensor histidine kinase YesM [Signal transduction mechanisms]; Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 41.54 E-value: 2.00e-03
|
||||||||||||
| PBP2_BsGlnH | cd13689 | Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ... |
35-252 | 2.43e-03 | ||||||||
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: 40.29 E-value: 2.43e-03
|
||||||||||||
| PBP2_GluR0 | cd00997 | Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ... |
54-117 | 3.29e-03 | ||||||||
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: 39.63 E-value: 3.29e-03
|
||||||||||||
| PBP2_AatB_like | cd00996 | Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong ... |
54-117 | 3.44e-03 | ||||||||
Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong to the type 2 periplasmic binding fold protein superfamily; This subfamily includes periplasmic binding domain of ATP-binding cassette transporter-like systems that serve as initial receptors in the ABC transport of amino acids and their derivatives in eubacteria. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The Abp proteins belong to the PBPI 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: 270217 [Multi-domain] Cd Length: 227 Bit Score: 39.87 E-value: 3.44e-03
|
||||||||||||
| PRK10604 | PRK10604 | sensor protein RstB; Provisional |
624-781 | 3.97e-03 | ||||||||
sensor protein RstB; Provisional Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 40.36 E-value: 3.97e-03
|
||||||||||||
| PksD | COG3321 | Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
224-758 | 4.56e-03 | ||||||||
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 40.63 E-value: 4.56e-03
|
||||||||||||
| HATPase_EvgS-ArcB-TorS-like | cd16922 | Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
702-782 | 4.89e-03 | ||||||||
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: 37.47 E-value: 4.89e-03
|
||||||||||||
| PBP2_GluB | cd13690 | Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ... |
26-252 | 4.90e-03 | ||||||||
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein fold; This group includes periplasmic glutamate-binding domain GluB from Corynebacterium efficiens and its related proteins. The GluB 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: 270408 [Multi-domain] Cd Length: 231 Bit Score: 39.17 E-value: 4.90e-03
|
||||||||||||
| COG3920 | COG3920 | Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ... |
150-442 | 6.16e-03 | ||||||||
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms]; Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 39.89 E-value: 6.16e-03
|
||||||||||||
| PAS | cd00130 | PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
335-426 | 8.56e-03 | ||||||||
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 36.46 E-value: 8.56e-03
|
||||||||||||
| HATPase_c_2 | pfam13581 | Histidine kinase-like ATPase domain; |
701-740 | 9.32e-03 | ||||||||
Histidine kinase-like ATPase domain; Pssm-ID: 433327 [Multi-domain] Cd Length: 127 Bit Score: 36.88 E-value: 9.32e-03
|
||||||||||||
| Blast search parameters | ||||
|
