SipW-dependent-type signal peptide-containing protein, partial [Gemmiger sp. An50]
Protein Classification
SipW-dependent-type signal peptide-containing protein( domain architecture ID 10024425)
SipW-dependent-type signal peptide-containing protein often found at N-terminus of CalY family proteins
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| cognate_SipW | TIGR04088 | SipW-cognate class signal peptide; This model describes a protein N-terminal domain found ... |
1-30 | 6.45e-04 | ||
SipW-cognate class signal peptide; This model describes a protein N-terminal domain found regularly in proteins encoded near a variant form of signal peptidase I such as the SipW protein of Bacillus subtilis. Many though not all members are homologs of camelysin (a casein-cleaving metalloprotease) and TasA (CotN), a metalloprotease that is secreted, along with extracellular polysaccharide (EPS), to be the major protein constituent of the Bacillus subtilis biofilm matrix. Sequencing from several known TasA/CotN proteins shows the cleavage location to be near the center of the alignment and typical of type I signal peptidases, with small residues at -3 and -1. This domain, therefore, appears to be a special subclass of signal peptide. : Pssm-ID: 274971 Cd Length: 34 Bit Score: 35.98 E-value: 6.45e-04
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| Name | Accession | Description | Interval | E-value | ||
| cognate_SipW | TIGR04088 | SipW-cognate class signal peptide; This model describes a protein N-terminal domain found ... |
1-30 | 6.45e-04 | ||
SipW-cognate class signal peptide; This model describes a protein N-terminal domain found regularly in proteins encoded near a variant form of signal peptidase I such as the SipW protein of Bacillus subtilis. Many though not all members are homologs of camelysin (a casein-cleaving metalloprotease) and TasA (CotN), a metalloprotease that is secreted, along with extracellular polysaccharide (EPS), to be the major protein constituent of the Bacillus subtilis biofilm matrix. Sequencing from several known TasA/CotN proteins shows the cleavage location to be near the center of the alignment and typical of type I signal peptidases, with small residues at -3 and -1. This domain, therefore, appears to be a special subclass of signal peptide. Pssm-ID: 274971 Cd Length: 34 Bit Score: 35.98 E-value: 6.45e-04
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| Name | Accession | Description | Interval | E-value | ||
| cognate_SipW | TIGR04088 | SipW-cognate class signal peptide; This model describes a protein N-terminal domain found ... |
1-30 | 6.45e-04 | ||
SipW-cognate class signal peptide; This model describes a protein N-terminal domain found regularly in proteins encoded near a variant form of signal peptidase I such as the SipW protein of Bacillus subtilis. Many though not all members are homologs of camelysin (a casein-cleaving metalloprotease) and TasA (CotN), a metalloprotease that is secreted, along with extracellular polysaccharide (EPS), to be the major protein constituent of the Bacillus subtilis biofilm matrix. Sequencing from several known TasA/CotN proteins shows the cleavage location to be near the center of the alignment and typical of type I signal peptidases, with small residues at -3 and -1. This domain, therefore, appears to be a special subclass of signal peptide. Pssm-ID: 274971 Cd Length: 34 Bit Score: 35.98 E-value: 6.45e-04
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