Domain

Subtilisin Carlsberg-like catalytic domain (IPR034202)

Short name: Subtilisin_Carlsberg-like

Domain relationships

Description

This entry includes prokaryote proteins with a subtilisin-like domain. Subtilisin is a serine endopeptidase in peptidase family S8, subfamily S8A [PMID: 8439290]. Characterized peptidases in this entry include subtilisin Carlsberg (S08.001), TK-subtilisin (S08.129), subtilisin PB92 (S08.003) and subtilisin BPN' (S08.034). TK-subtilisin is secreted from the hyperthermophilic archaeon Thermococcus kodakaraensis as an inactive precursor. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity, unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain, unlike the bacterial subtilases, because of the stability produced from Ca2+ binding [PMID: 19766655, PMID: 18951896]. Subtilisin BPN'/Novo is extremely similar in structure to subtilisin Carlsberg though it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and two possible Ca2+ binding sites have been identified [PMID: 9552156, PMID: 3150541]. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents [PMID: 3537081]. Subtilisin Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins [PMID: 9115441].

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.
CDD
  • cd07477 (Peptidases_S8_Subtilisin_subse)