| Description | This entry includes zinc-dependent metalloprotease domains from the serralysin and related proteins such as PbrA from Pseudomonas [ ]. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in Gram-negative bacteria, that does not require N-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain C-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel β roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides [, , ]. | Name | Serralysin-like metallopeptidase domain |
| Short Name | Serralysin-like | Type | Domain |
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