Pathways & interactions
Vpr-like peptidase, catalytic domain (IPR034213)
Short name: S8_Vpr-like
Overlapping homologous superfamilies
- Peptidase S8/S53 domain superfamily (IPR036852)
- Peptidase S8/S53 domain (IPR000209)
- Vpr-like peptidase, catalytic domain (IPR034213)
This entry represents a peptidase Vpr-like domain, found in a subgroup of proteins that belong to the peptidase family S8, subfamily S8A (subtilisin) [PMID: 8439290]. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes post-translational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr (MEROPS identifier S08.114) was identified as one of the endopeptidases, along with WprA and AprE, that are capable of processing subtilin [PMID: 12705882]. Vpr is secreted and synthesized as an auto-processing precursor, and has been shown to be fibrinolytic [PMID: 15596354]. This entry also includes the FT peptidase from Bacillus sp. KSM-KP43 (S08.117) [PMID: 14642820].
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].
- cd07474 (Peptidases_S8_subtilisin_Vpr-l)