MULTISPECIES: chaplin [Streptomyces]
chaplin( domain architecture ID 10510227)
chaplin is a small secreted Streptomycete protein involved in the formation of aerial hyphae
List of domain hits
Name | Accession | Description | Interval | E-value | ||
ChpA-C | pfam03777 | ChpA-C; Small domain found in a family of secreted streptomyces proteins. It occurs singly or ... |
32-78 | 3.71e-22 | ||
ChpA-C; Small domain found in a family of secreted streptomyces proteins. It occurs singly or as a pair. Many of the domains have two cysteines that may form a disulphide bridge. This domain is found in chaplins ChpA-C (coelicolor hydrophobic aerial) proteins. ChpA-C contain a canonical C-terminal sortase signal, which is recognized by sortase enzymes that covalently couple their substrates to the peptidoglycan present in the cell wall. Indeed, direct evidence for sortase-mediated coupling of ChpC has been demonstrated, and it is expected that ChpA and ChpB are also anchored to the cell wall. : Pssm-ID: 397719 [Multi-domain] Cd Length: 55 Bit Score: 81.14 E-value: 3.71e-22
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Name | Accession | Description | Interval | E-value | ||
ChpA-C | pfam03777 | ChpA-C; Small domain found in a family of secreted streptomyces proteins. It occurs singly or ... |
32-78 | 3.71e-22 | ||
ChpA-C; Small domain found in a family of secreted streptomyces proteins. It occurs singly or as a pair. Many of the domains have two cysteines that may form a disulphide bridge. This domain is found in chaplins ChpA-C (coelicolor hydrophobic aerial) proteins. ChpA-C contain a canonical C-terminal sortase signal, which is recognized by sortase enzymes that covalently couple their substrates to the peptidoglycan present in the cell wall. Indeed, direct evidence for sortase-mediated coupling of ChpC has been demonstrated, and it is expected that ChpA and ChpB are also anchored to the cell wall. Pssm-ID: 397719 [Multi-domain] Cd Length: 55 Bit Score: 81.14 E-value: 3.71e-22
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Name | Accession | Description | Interval | E-value | ||
ChpA-C | pfam03777 | ChpA-C; Small domain found in a family of secreted streptomyces proteins. It occurs singly or ... |
32-78 | 3.71e-22 | ||
ChpA-C; Small domain found in a family of secreted streptomyces proteins. It occurs singly or as a pair. Many of the domains have two cysteines that may form a disulphide bridge. This domain is found in chaplins ChpA-C (coelicolor hydrophobic aerial) proteins. ChpA-C contain a canonical C-terminal sortase signal, which is recognized by sortase enzymes that covalently couple their substrates to the peptidoglycan present in the cell wall. Indeed, direct evidence for sortase-mediated coupling of ChpC has been demonstrated, and it is expected that ChpA and ChpB are also anchored to the cell wall. Pssm-ID: 397719 [Multi-domain] Cd Length: 55 Bit Score: 81.14 E-value: 3.71e-22
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