ESPR domain-containing protein, partial [Salmonella enterica]
Protein Classification
ESPR domain-containing protein( domain architecture ID 10585893)
ESPR (Extended Signal Peptide Region) domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| ESPR | pfam13018 | Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ... |
1-36 | 7.03e-09 | ||
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: 45.99 E-value: 7.03e-09
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| Name | Accession | Description | Interval | E-value | ||
| ESPR | pfam13018 | Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ... |
1-36 | 7.03e-09 | ||
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: 45.99 E-value: 7.03e-09
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| Name | Accession | Description | Interval | E-value | ||
| ESPR | pfam13018 | Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ... |
1-36 | 7.03e-09 | ||
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: 45.99 E-value: 7.03e-09
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