Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ...
1-50
7.25e-10
Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N-terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). So far, the ESPR is present only in Gram-negative bacterial proteins originating from the classes Beta- and Gamma-proteobacteria. ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation. Deletion of ESPR causes mis-folding of the TAAs passenger domain in the periplasm, substantially impairing its translocation across the outer membrane.
Pssm-ID: 463773 [Multi-domain] Cd Length: 50 Bit Score: 54.46 E-value: 7.25e-10
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
63-543
5.12e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 59.49 E-value: 5.12e-09
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
196-258
4.77e-08
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 51.73 E-value: 4.77e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
304-465
5.33e-06
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 49.48 E-value: 5.33e-06
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
467-543
1.30e-05
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 48.32 E-value: 1.30e-05
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
467-543
1.50e-04
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 44.86 E-value: 1.50e-04
Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ...
1-50
7.25e-10
Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N-terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). So far, the ESPR is present only in Gram-negative bacterial proteins originating from the classes Beta- and Gamma-proteobacteria. ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation. Deletion of ESPR causes mis-folding of the TAAs passenger domain in the periplasm, substantially impairing its translocation across the outer membrane.
Pssm-ID: 463773 [Multi-domain] Cd Length: 50 Bit Score: 54.46 E-value: 7.25e-10
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
63-543
5.12e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 59.49 E-value: 5.12e-09
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
196-258
4.77e-08
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 51.73 E-value: 4.77e-08
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
196-259
8.52e-08
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 50.96 E-value: 8.52e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
304-465
5.33e-06
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 49.48 E-value: 5.33e-06
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
467-543
1.30e-05
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 48.32 E-value: 1.30e-05
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
205-258
2.57e-05
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 44.02 E-value: 2.57e-05
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
467-543
1.50e-04
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 44.86 E-value: 1.50e-04
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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