SusC/RagA family TonB-linked outer membrane protein might act as a TonB-dependent receptor similar to Bacteroides thetaiotaomicron starch-utilization system protein C (SusC), which mediates transport of starch oligosaccharides from the surface of the outer membrane to the periplasm for subsequent degradation
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade ...
30-1048
0e+00
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate]
:
Pssm-ID: 274948 [Multi-domain] Cd Length: 981 Bit Score: 818.37 E-value: 0e+00
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade ...
30-1048
0e+00
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 274948 [Multi-domain] Cd Length: 981 Bit Score: 818.37 E-value: 0e+00
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
31-112
4.13e-20
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.
Pssm-ID: 433425 [Multi-domain] Cd Length: 88 Bit Score: 85.72 E-value: 4.13e-20
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ...
127-450
2.14e-07
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.
Pssm-ID: 238657 [Multi-domain] Cd Length: 635 Bit Score: 55.15 E-value: 2.14e-07
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade ...
30-1048
0e+00
TonB-linked outer membrane protein, SusC/RagA family; This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 274948 [Multi-domain] Cd Length: 981 Bit Score: 818.37 E-value: 0e+00
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
31-112
4.13e-20
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.
Pssm-ID: 433425 [Multi-domain] Cd Length: 88 Bit Score: 85.72 E-value: 4.13e-20
TonB-dependent Receptor Plug Domain; The Plug domain has been shown to be an independently ...
122-221
2.13e-13
TonB-dependent Receptor Plug Domain; The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors. It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel.
Pssm-ID: 462243 [Multi-domain] Cd Length: 107 Bit Score: 67.29 E-value: 2.13e-13
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ...
127-450
2.14e-07
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.
Pssm-ID: 238657 [Multi-domain] Cd Length: 635 Bit Score: 55.15 E-value: 2.14e-07
TonB-dependent outer membrane receptor, SusC/RagA subfamily, signature region; This model ...
199-228
2.55e-07
TonB-dependent outer membrane receptor, SusC/RagA subfamily, signature region; This model describes a 31-residue signature region of the SusC/RagA family of outer membrane proteins from the Bacteriodetes. While many TonB-dependent outer membrane receptors are associated with siderophore import, this family seems to include generalized nutrient receptors that may convey fairly large oligomers of protein or carbohydrate. This family occurs in high copy numbers in the most abundant species of the human gut microbiome.
Pssm-ID: 274949 [Multi-domain] Cd Length: 31 Bit Score: 47.57 E-value: 2.55e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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