autotransporter outer membrane beta-barrel domain-containing protein similar to Bordetella pertactin autotransporter, an agglutinogen that binds to eukaryotic cells, which may have a role in bacterial adhesion, and thus play a role in virulence
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ...
427-870
6.15e-113
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: 352.07 E-value: 6.15e-113
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of ...
287-530
5.64e-59
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of Neisseria and Haemophilus IgA1 proteases, SPATEs (serine protease autotransporters secreted by Enterobacteriaceae), Bordetella pertacins, and nonprotease autotransporters, TibA and similar AIDA-like proteins.
:
Pssm-ID: 238653 [Multi-domain] Cd Length: 233 Bit Score: 201.04 E-value: 5.64e-59
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ...
427-870
6.15e-113
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: 352.07 E-value: 6.15e-113
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of ...
287-530
5.64e-59
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of Neisseria and Haemophilus IgA1 proteases, SPATEs (serine protease autotransporters secreted by Enterobacteriaceae), Bordetella pertacins, and nonprotease autotransporters, TibA and similar AIDA-like proteins.
Pssm-ID: 238653 [Multi-domain] Cd Length: 233 Bit Score: 201.04 E-value: 5.64e-59
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
611-853
4.11e-39
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: 146.18 E-value: 4.11e-39
Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V ...
345-530
7.36e-29
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: 114.00 E-value: 7.36e-29
BafA family autotransporter C-terminal domain; BafA from both Bartonella henselae and ...
412-869
1.42e-25
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: 112.81 E-value: 1.42e-25
outer membrane autotransporter barrel domain; A number of Gram-negative bacterial proteins, ...
427-870
6.15e-113
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: 352.07 E-value: 6.15e-113
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of ...
287-530
5.64e-59
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 1, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of Neisseria and Haemophilus IgA1 proteases, SPATEs (serine protease autotransporters secreted by Enterobacteriaceae), Bordetella pertacins, and nonprotease autotransporters, TibA and similar AIDA-like proteins.
Pssm-ID: 238653 [Multi-domain] Cd Length: 233 Bit Score: 201.04 E-value: 5.64e-59
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
609-849
3.34e-45
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: 163.32 E-value: 3.34e-45
Autotransporter beta-domain; Secretion of protein products occurs by a number of different ...
611-853
4.11e-39
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: 146.18 E-value: 4.11e-39
Pertactin-like passenger domains (virulence factors) of autotransporter proteins of the type V ...
345-530
7.36e-29
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: 114.00 E-value: 7.36e-29
BafA family autotransporter C-terminal domain; BafA from both Bartonella henselae and ...
412-869
1.42e-25
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: 112.81 E-value: 1.42e-25
Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 2, of ...
345-520
1.39e-07
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: 52.69 E-value: 1.39e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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