LacI family DNA-binding transcriptional regulator [Xanthomonas euvesicatoria]
Protein Classification
LacI family DNA-binding transcriptional regulator( domain architecture ID 11265679)
LacI family DNA-binding transcriptional regulator functions as an activator or repressor by binding a specific effector ligand that either decreases (induction) or increases DNA-binding affinity (co-repression)
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PBP1_SalR | cd01545 | ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
72-343 | 7.06e-112 | |||||
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. : Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 326.43 E-value: 7.06e-112
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| HTH_LACI | smart00354 | helix_turn _helix lactose operon repressor; |
13-79 | 5.28e-20 | |||||
helix_turn _helix lactose operon repressor; : Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 82.63 E-value: 5.28e-20
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| Name | Accession | Description | Interval | E-value | ||||||
| PBP1_SalR | cd01545 | ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
72-343 | 7.06e-112 | ||||||
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 326.43 E-value: 7.06e-112
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| PurR | COG1609 | DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
10-348 | 2.67e-110 | ||||||
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 324.84 E-value: 2.67e-110
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| lacI | PRK09526 | lac repressor; Reviewed |
12-345 | 5.82e-62 | ||||||
lac repressor; Reviewed Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 201.38 E-value: 5.82e-62
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| Peripla_BP_3 | pfam13377 | Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
181-344 | 4.46e-35 | ||||||
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 125.53 E-value: 4.46e-35
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| HTH_LACI | smart00354 | helix_turn _helix lactose operon repressor; |
13-79 | 5.28e-20 | ||||||
helix_turn _helix lactose operon repressor; Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 82.63 E-value: 5.28e-20
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| HTH_LacI | cd01392 | Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
17-67 | 1.31e-17 | ||||||
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites. Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 75.52 E-value: 1.31e-17
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| LacI | pfam00356 | Bacterial regulatory proteins, lacI family; |
14-59 | 1.48e-13 | ||||||
Bacterial regulatory proteins, lacI family; Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 64.20 E-value: 1.48e-13
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| Name | Accession | Description | Interval | E-value | ||||||
| PBP1_SalR | cd01545 | ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
72-343 | 7.06e-112 | ||||||
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 326.43 E-value: 7.06e-112
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| PurR | COG1609 | DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
10-348 | 2.67e-110 | ||||||
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 324.84 E-value: 2.67e-110
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| PBP1_LacI_sugar_binding-like | cd06267 | ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
73-339 | 8.07e-74 | ||||||
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain. Pssm-ID: 380491 [Multi-domain] Cd Length: 264 Bit Score: 229.33 E-value: 8.07e-74
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| PBP1_LacI-like | cd06284 | ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
126-343 | 1.30e-68 | ||||||
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding. Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 215.87 E-value: 1.30e-68
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| PBP1_LacI-like | cd06285 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
73-344 | 2.70e-64 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 205.15 E-value: 2.70e-64
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| lacI | PRK09526 | lac repressor; Reviewed |
12-345 | 5.82e-62 | ||||||
lac repressor; Reviewed Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 201.38 E-value: 5.82e-62
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| PBP1_CcpA-like | cd19975 | ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
73-343 | 7.45e-61 | ||||||
ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators. Pssm-ID: 380630 [Multi-domain] Cd Length: 269 Bit Score: 196.24 E-value: 7.45e-61
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| PBP1_CatR-like | cd06296 | ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
72-344 | 7.29e-60 | ||||||
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380519 [Multi-domain] Cd Length: 270 Bit Score: 193.65 E-value: 7.29e-60
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| PBP1_LacI-like | cd06278 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
73-343 | 5.03e-57 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 186.20 E-value: 5.03e-57
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| PBP1_LacI | cd01574 | ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
117-343 | 7.88e-56 | ||||||
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380488 [Multi-domain] Cd Length: 265 Bit Score: 183.17 E-value: 7.88e-56
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| PBP1_GalS-like | cd06270 | ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
73-341 | 1.00e-55 | ||||||
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems. Pssm-ID: 380494 [Multi-domain] Cd Length: 266 Bit Score: 182.72 E-value: 1.00e-55
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| PBP1_PurR | cd06275 | ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
73-343 | 3.89e-55 | ||||||
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380499 [Multi-domain] Cd Length: 269 Bit Score: 181.30 E-value: 3.89e-55
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| PRK10703 | PRK10703 | HTH-type transcriptional repressor PurR; |
13-349 | 4.30e-55 | ||||||
HTH-type transcriptional repressor PurR; Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 183.39 E-value: 4.30e-55
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| PBP1_sucrose_transcription_regulator | cd06288 | ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
119-343 | 6.40e-55 | ||||||
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 180.82 E-value: 6.40e-55
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| PBP1_AglR_RafR-like | cd06292 | Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
81-344 | 3.02e-54 | ||||||
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380515 [Multi-domain] Cd Length: 273 Bit Score: 179.39 E-value: 3.02e-54
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| PBP1_LacI-like | cd06290 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
73-316 | 5.52e-53 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 175.88 E-value: 5.52e-53
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| PBP1_EndR-like | cd19977 | periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
121-326 | 1.29e-52 | ||||||
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding. Pssm-ID: 380632 [Multi-domain] Cd Length: 264 Bit Score: 174.64 E-value: 1.29e-52
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| PBP1_LacI-like | cd06273 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
117-343 | 8.66e-51 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 170.00 E-value: 8.66e-51
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| PBP1_LacI-like | cd06280 | ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
111-323 | 1.07e-50 | ||||||
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding. Pssm-ID: 380503 [Multi-domain] Cd Length: 266 Bit Score: 169.75 E-value: 1.07e-50
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| PBP1_Qymf-like | cd06291 | ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
126-343 | 2.33e-50 | ||||||
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 168.85 E-value: 2.33e-50
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| PRK10423 | PRK10423 | transcriptional repressor RbsR; Provisional |
17-343 | 2.16e-49 | ||||||
transcriptional repressor RbsR; Provisional Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 168.34 E-value: 2.16e-49
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| PBP1_LacI-like | cd06293 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
119-343 | 3.43e-49 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 165.91 E-value: 3.43e-49
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| PBP1_MalI-like | cd06289 | ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
114-341 | 7.00e-49 | ||||||
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 165.05 E-value: 7.00e-49
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| PBP1_LacI-like | cd06279 | ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
117-343 | 6.64e-48 | ||||||
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding. Pssm-ID: 380502 [Multi-domain] Cd Length: 284 Bit Score: 163.15 E-value: 6.64e-48
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| PBP1_DegA_Like | cd19976 | ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
119-343 | 8.18e-48 | ||||||
ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding. Pssm-ID: 380631 [Multi-domain] Cd Length: 268 Bit Score: 162.42 E-value: 8.18e-48
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| PRK11041 | PRK11041 | DNA-binding transcriptional regulator CytR; Provisional |
39-348 | 2.27e-47 | ||||||
DNA-binding transcriptional regulator CytR; Provisional Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 162.47 E-value: 2.27e-47
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| PBP1_AglR-like | cd20010 | Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
73-339 | 3.84e-45 | ||||||
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380665 [Multi-domain] Cd Length: 269 Bit Score: 155.40 E-value: 3.84e-45
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| PBP1_AraR | cd01541 | ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
119-343 | 4.05e-45 | ||||||
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380483 [Multi-domain] Cd Length: 274 Bit Score: 155.41 E-value: 4.05e-45
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| PBP1_GalR | cd01544 | ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
122-343 | 4.45e-44 | ||||||
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems. Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 152.68 E-value: 4.45e-44
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| PBP1_LacI-like | cd06299 | ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
73-343 | 7.59e-44 | ||||||
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380522 [Multi-domain] Cd Length: 268 Bit Score: 152.05 E-value: 7.59e-44
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| PBP1_GntR | cd01575 | ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
121-343 | 1.94e-41 | ||||||
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380489 [Multi-domain] Cd Length: 269 Bit Score: 145.72 E-value: 1.94e-41
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| PBP1_LacI-like | cd06277 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
126-343 | 1.37e-39 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 141.22 E-value: 1.37e-39
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| PBP1_LacI-like | cd06282 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
114-321 | 3.85e-39 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 139.73 E-value: 3.85e-39
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| PBP1_CcpB-like | cd06286 | ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
72-341 | 2.68e-38 | ||||||
ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree. Pssm-ID: 380509 [Multi-domain] Cd Length: 262 Bit Score: 137.29 E-value: 2.68e-38
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| PBP1_TreR-like | cd01542 | ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
125-339 | 3.38e-38 | ||||||
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 136.86 E-value: 3.38e-38
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| PBP1_MalR-like | cd06294 | ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
73-339 | 3.49e-38 | ||||||
ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380517 [Multi-domain] Cd Length: 269 Bit Score: 137.33 E-value: 3.49e-38
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| PBP1_LacI-like | cd06281 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
125-343 | 2.26e-37 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 135.06 E-value: 2.26e-37
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| PBP1_LacI-like | cd19974 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
126-343 | 2.96e-36 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380629 [Multi-domain] Cd Length: 270 Bit Score: 132.29 E-value: 2.96e-36
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| PRK10014 | PRK10014 | DNA-binding transcriptional repressor MalI; Provisional |
1-342 | 7.91e-36 | ||||||
DNA-binding transcriptional repressor MalI; Provisional Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 132.91 E-value: 7.91e-36
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| Peripla_BP_3 | pfam13377 | Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
181-344 | 4.46e-35 | ||||||
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 125.53 E-value: 4.46e-35
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| PBP1_CcpA | cd06298 | ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
121-343 | 1.24e-34 | ||||||
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators. Pssm-ID: 380521 [Multi-domain] Cd Length: 268 Bit Score: 127.79 E-value: 1.24e-34
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| PBP1_CelR | cd06295 | ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
125-316 | 8.74e-34 | ||||||
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380518 [Multi-domain] Cd Length: 273 Bit Score: 125.83 E-value: 8.74e-34
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| PRK10727 | PRK10727 | HTH-type transcriptional regulator GalR; |
13-348 | 2.52e-33 | ||||||
HTH-type transcriptional regulator GalR; Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 126.02 E-value: 2.52e-33
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| PBP1_repressor_sugar_binding-like | cd01537 | Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
72-322 | 4.77e-33 | ||||||
Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor. Pssm-ID: 380479 [Multi-domain] Cd Length: 265 Bit Score: 123.51 E-value: 4.77e-33
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| PRK14987 | PRK14987 | HTH-type transcriptional regulator GntR; |
15-319 | 4.33e-30 | ||||||
HTH-type transcriptional regulator GntR; Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 117.43 E-value: 4.33e-30
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| PBP1_RegR_EndR_KdgR-like | cd06283 | ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
73-321 | 9.33e-30 | ||||||
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380506 [Multi-domain] Cd Length: 266 Bit Score: 114.57 E-value: 9.33e-30
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| PRK10401 | PRK10401 | HTH-type transcriptional regulator GalS; |
14-345 | 5.50e-27 | ||||||
HTH-type transcriptional regulator GalS; Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 109.10 E-value: 5.50e-27
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| PBP1_CcpA_TTHA0807 | cd06297 | ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
151-319 | 7.54e-27 | ||||||
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators. Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 107.17 E-value: 7.54e-27
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| PBP1_hexuronate_repressor-like | cd06272 | ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
126-326 | 8.90e-27 | ||||||
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380496 [Multi-domain] Cd Length: 266 Bit Score: 106.69 E-value: 8.90e-27
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| PBP1_XylR | cd01543 | ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
112-344 | 3.43e-25 | ||||||
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380485 [Multi-domain] Cd Length: 265 Bit Score: 102.28 E-value: 3.43e-25
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| PBP1_AglR_RafR-like | cd06271 | ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
126-318 | 1.64e-24 | ||||||
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 100.58 E-value: 1.64e-24
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| PRK10339 | PRK10339 | DNA-binding transcriptional repressor EbgR; Provisional |
13-344 | 3.32e-23 | ||||||
DNA-binding transcriptional repressor EbgR; Provisional Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 98.29 E-value: 3.32e-23
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| PBP1_RafR-like | cd20009 | Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
114-335 | 1.43e-21 | ||||||
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380664 [Multi-domain] Cd Length: 266 Bit Score: 92.60 E-value: 1.43e-21
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| HTH_LACI | smart00354 | helix_turn _helix lactose operon repressor; |
13-79 | 5.28e-20 | ||||||
helix_turn _helix lactose operon repressor; Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 82.63 E-value: 5.28e-20
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| RbsB | COG1879 | ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
61-333 | 8.08e-20 | ||||||
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism]; Pssm-ID: 441483 [Multi-domain] Cd Length: 307 Bit Score: 88.44 E-value: 8.08e-20
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| Peripla_BP_1 | pfam00532 | Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
73-324 | 4.72e-19 | ||||||
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356). Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 85.64 E-value: 4.72e-19
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| PBP1_ABC_sugar_binding-like | cd01536 | periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
119-319 | 1.31e-17 | ||||||
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins. Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 81.46 E-value: 1.31e-17
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| HTH_LacI | cd01392 | Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
17-67 | 1.31e-17 | ||||||
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites. Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 75.52 E-value: 1.31e-17
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| PBP1_FruR | cd06274 | ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
114-334 | 1.32e-16 | ||||||
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 78.40 E-value: 1.32e-16
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| PRK11303 | PRK11303 | catabolite repressor/activator; |
14-253 | 3.53e-16 | ||||||
catabolite repressor/activator; Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 78.38 E-value: 3.53e-16
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| PBP1_ABC_sugar_binding-like | cd06319 | periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
121-328 | 1.27e-15 | ||||||
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 75.86 E-value: 1.27e-15
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| Peripla_BP_4 | pfam13407 | Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
73-319 | 1.01e-13 | ||||||
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 70.03 E-value: 1.01e-13
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| LacI | pfam00356 | Bacterial regulatory proteins, lacI family; |
14-59 | 1.48e-13 | ||||||
Bacterial regulatory proteins, lacI family; Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 64.20 E-value: 1.48e-13
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| Periplasmic_Binding_Protein_type1 | cd01391 | Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
98-317 | 1.80e-13 | ||||||
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold. Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 69.61 E-value: 1.80e-13
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| PBP1_ABC_IbpA-like | cd19968 | periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
119-327 | 5.72e-13 | ||||||
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 68.18 E-value: 5.72e-13
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| PBP1_ABC_sugar_binding-like | cd06310 | monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
114-287 | 3.08e-11 | ||||||
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 63.13 E-value: 3.08e-11
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| PBP1_TmRBP-like | cd19967 | D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
119-311 | 3.73e-11 | ||||||
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability. Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 62.72 E-value: 3.73e-11
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| PBP1_LacI-like | cd06287 | ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
126-343 | 3.80e-10 | ||||||
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor. Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 59.74 E-value: 3.80e-10
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| PBP1_sensor_kinase-like | cd06308 | periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
119-259 | 4.86e-10 | ||||||
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail. Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 59.48 E-value: 4.86e-10
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| PBP1_galactofuranose_YtfQ-like | cd06309 | periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
121-339 | 9.33e-10 | ||||||
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally. Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 58.77 E-value: 9.33e-10
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| PBP1_ABC_sugar_binding-like | cd20004 | monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
119-319 | 9.67e-10 | ||||||
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 58.78 E-value: 9.67e-10
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| PBP1_ABC_sugar_binding-like | cd19970 | monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
119-289 | 9.69e-09 | ||||||
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 55.72 E-value: 9.69e-09
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| PBP1_ABC_sugar_binding-like | cd06324 | periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
119-289 | 1.03e-08 | ||||||
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 55.69 E-value: 1.03e-08
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| PBP1_ABC_sugar_binding-like | cd06317 | periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
72-320 | 4.48e-08 | ||||||
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 53.53 E-value: 4.48e-08
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| PBP1_sugar_binding | cd06307 | periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
122-256 | 9.77e-08 | ||||||
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes. Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 52.56 E-value: 9.77e-08
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| PBP1_ABC_sugar_binding-like | cd06322 | periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
114-289 | 1.01e-07 | ||||||
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 52.66 E-value: 1.01e-07
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| PBP1_ABC_sugar_binding-like | cd20006 | monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
111-289 | 2.12e-07 | ||||||
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 51.44 E-value: 2.12e-07
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| PBP1_rhizopine_binding-like | cd06301 | periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
119-320 | 6.37e-06 | ||||||
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily. Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 47.23 E-value: 6.37e-06
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| PBP1_ABC_sugar_binding-like | cd19972 | monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
73-311 | 1.21e-05 | ||||||
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 46.28 E-value: 1.21e-05
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| PBP1_ABC_sugar_binding-like | cd19971 | monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
119-259 | 1.28e-05 | ||||||
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 46.04 E-value: 1.28e-05
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| PBP1_ribose_binding | cd06323 | periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
119-328 | 1.47e-05 | ||||||
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability. Pssm-ID: 380546 [Multi-domain] Cd Length: 268 Bit Score: 45.75 E-value: 1.47e-05
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| PBP1_tmGBP | cd06314 | periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
119-318 | 1.79e-05 | ||||||
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP). Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 45.65 E-value: 1.79e-05
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| PBP1_ABC_sugar_binding-like | cd06321 | periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
119-289 | 2.86e-05 | ||||||
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 44.97 E-value: 2.86e-05
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| PBP1_ABC_D-talitol-like | cd06318 | periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
119-323 | 4.24e-05 | ||||||
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 44.71 E-value: 4.24e-05
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| PBP1_allose_binding | cd06320 | periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
119-319 | 4.94e-05 | ||||||
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 44.56 E-value: 4.94e-05
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| PBP1_ABC_xylose_binding-like | cd19992 | periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
119-259 | 7.10e-05 | ||||||
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 43.73 E-value: 7.10e-05
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| PBP1_TorT-like | cd06306 | TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
119-222 | 1.10e-04 | ||||||
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport. Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 43.34 E-value: 1.10e-04
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| PBP1_ABC_sugar_binding-like | cd20005 | monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
122-319 | 1.30e-04 | ||||||
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 43.00 E-value: 1.30e-04
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| PBP1_ABC_sugar_binding-like | cd06311 | periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
114-259 | 1.63e-04 | ||||||
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 42.74 E-value: 1.63e-04
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| PBP1_ABC_sugar_binding-like | cd19969 | monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
113-287 | 4.18e-04 | ||||||
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis. Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 41.55 E-value: 4.18e-04
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| PBP1_ABC_sugar_binding-like | cd06300 | periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
94-213 | 2.68e-03 | ||||||
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail. Pssm-ID: 380523 [Multi-domain] Cd Length: 302 Bit Score: 39.23 E-value: 2.68e-03
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| PBP1_ABC_sugar_binding-like | cd19999 | monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
121-213 | 5.47e-03 | ||||||
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail. Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 38.06 E-value: 5.47e-03
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