autotransporter outer membrane beta-barrel domain-containing protein similar to Escherichia coli uncharacterized protein YaiT and Bordetella pertussis autotransporter BrkA (Bordetella serum-resistance killing protein A)
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ...
580-992
1.52e-74
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
:
Pssm-ID: 273608 [Multi-domain] Cd Length: 431 Bit Score: 252.30 E-value: 1.52e-74
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ...
580-992
1.52e-74
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 273608 [Multi-domain] Cd Length: 431 Bit Score: 252.30 E-value: 1.52e-74
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
734-971
8.09e-36
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs.
Pssm-ID: 461054 [Multi-domain] Cd Length: 255 Bit Score: 136.74 E-value: 8.09e-36
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
736-981
8.44e-29
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
Pssm-ID: 214872 [Multi-domain] Cd Length: 268 Bit Score: 116.51 E-value: 8.44e-29
BafA family autotransporter C-terminal domain; BafA from both Bartonella henselae and ...
748-990
2.99e-19
BafA family autotransporter C-terminal domain; BafA from both Bartonella henselae and Bartonella quintana, and possibly all Bartonella BafA, are mitogenic autotransporter virulence factors that help induce vasoproliferative lesions during infection. This HMM represents the more conserved C-terminal portion only, as the passenger region is more highly variable in length and sequence.
Pssm-ID: 468508 [Multi-domain] Cd Length: 617 Bit Score: 93.17 E-value: 2.99e-19
Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V ...
527-684
1.21e-09
Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V secretion system. Autotransporters are proteins used by Gram-negative bacteria to transport proteins across their outer membranes. The C-terminal (beta) domain of autotransporters forms a pore in the outer membrane through which the N-terminal passenger domain is transported. Following transport, the passenger domain is generally cleaved by an outer membrane protease with the passenger domain either remaining in contact with the surface via a noncovalent interaction with the beta domain or cleaved to release a soluble protein. These proteins are highly diverse and perform a variety of functions that promote virulence, including catalyzing proteolysis, serving as an adhesin, mediating actin-promoted motility, or serving as a cytotoxin. Proteins in this family share similarity in the C-terminal region of the passenger domain as seen in the pertactin structure P.69, a Bordetella pertussis agglutinogen responsible for human pertussis. The P.69 protein consists of a 16-stranded parallel beta-helix with a V-shaped cross-section, and is one of the largest beta-helix known to date.
Pssm-ID: 238156 [Multi-domain] Cd Length: 186 Bit Score: 58.53 E-value: 1.21e-09
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ...
580-992
1.52e-74
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, mostly found in pathogens and associated with virulence, contain a conserved C-terminal domain that integrates into the outer membrane and enables the N-terminal region to be delivered across the membrane. This C-terminal autotransporter domain is about 400 amino acids in length and includes the aromatic amino acid-rich OMP signal, typically ending with a Phe or Trp residue, at the extreme C-terminus. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 273608 [Multi-domain] Cd Length: 431 Bit Score: 252.30 E-value: 1.52e-74
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
734-971
8.09e-36
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs.
Pssm-ID: 461054 [Multi-domain] Cd Length: 255 Bit Score: 136.74 E-value: 8.09e-36
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
736-981
8.44e-29
Autotransporter beta-domain; Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.
Pssm-ID: 214872 [Multi-domain] Cd Length: 268 Bit Score: 116.51 E-value: 8.44e-29
BafA family autotransporter C-terminal domain; BafA from both Bartonella henselae and ...
748-990
2.99e-19
BafA family autotransporter C-terminal domain; BafA from both Bartonella henselae and Bartonella quintana, and possibly all Bartonella BafA, are mitogenic autotransporter virulence factors that help induce vasoproliferative lesions during infection. This HMM represents the more conserved C-terminal portion only, as the passenger region is more highly variable in length and sequence.
Pssm-ID: 468508 [Multi-domain] Cd Length: 617 Bit Score: 93.17 E-value: 2.99e-19
Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V ...
527-684
1.21e-09
Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V secretion system. Autotransporters are proteins used by Gram-negative bacteria to transport proteins across their outer membranes. The C-terminal (beta) domain of autotransporters forms a pore in the outer membrane through which the N-terminal passenger domain is transported. Following transport, the passenger domain is generally cleaved by an outer membrane protease with the passenger domain either remaining in contact with the surface via a noncovalent interaction with the beta domain or cleaved to release a soluble protein. These proteins are highly diverse and perform a variety of functions that promote virulence, including catalyzing proteolysis, serving as an adhesin, mediating actin-promoted motility, or serving as a cytotoxin. Proteins in this family share similarity in the C-terminal region of the passenger domain as seen in the pertactin structure P.69, a Bordetella pertussis agglutinogen responsible for human pertussis. The P.69 protein consists of a 16-stranded parallel beta-helix with a V-shaped cross-section, and is one of the largest beta-helix known to date.
Pssm-ID: 238156 [Multi-domain] Cd Length: 186 Bit Score: 58.53 E-value: 1.21e-09
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 2, of ...
510-682
3.56e-04
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 2, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of the nonprotease autotransporters, Ag43, AIDA-1 and IcsA, as well as, the less characterized ShdA, MisL, and BapA autotransporters.
Pssm-ID: 238654 [Multi-domain] Cd Length: 188 Bit Score: 42.67 E-value: 3.56e-04
Outer membrane protein beta-barrel domain; This domain is found in a wide range of outer ...
837-989
1.56e-03
Outer membrane protein beta-barrel domain; This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.
Pssm-ID: 463903 [Multi-domain] Cd Length: 175 Bit Score: 40.46 E-value: 1.56e-03
TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) ...
548-886
6.71e-03
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: 40.13 E-value: 6.71e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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