Peptidase MprA-like catalytic domain (IPR034176)

Short name: Peptidases_S8_13

Overlapping homologous superfamilies

Domain relationships


This entry represents a peptidase MprA-like domain, found in the bacterial members of the peptidase family S8 (subtilase serine endo- and exo-peptidases) [PMID: 8439290], including peptidase MprA from Burkholderia (MEROPS identifier S08.107) which degrades host immunoglobulins, transferrin and myosin [PMID: 22919676]; apr (S08.023, S08.040, S08.067) and bpr peptidases (S08.022) from Dichelobacter, which break down collagen in sheep hooves (ovine foot-rot) [PMID: 20208163]; StmPr1 peptidase from Stenotrophomonas (S08.110) which is a keratinase. These enzymes are stabilized by calcium ions, and because of sensitivity to EDTA were erronerously considered to be metallopeptidases [PMID: 11040430, PMID: 26896861].

The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subtilises are presently known, more than 170 of which with their complete amino acid sequence [PMID: 9070434]. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses [PMID: 7845208]. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [PMID: 7845208, PMID: 8439290]. Structures have been determined for several members of the subtilisin family: they exploit the same catalytic triad as the chymotrypsins, although the residues occur in a different order (HDS in chymotrypsin and DHS in subtilisin), but the structures show no other similarity [PMID: 7845208, PMID: 8439290]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein [PMID: 7845208].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.