Homologous Superfamily

Serralysin-like metalloprotease, C-terminal (IPR011049)

Short name: Serralysin-like_metalloprot_C

Overlapping entries


Serralysin is a bacterial Zn-endopeptidase that acts as a virulence factor to cause tissue damage and anaphylactic response [PMID: 12072965]. Many Zn-endopeptidases contain the metal binding motif HexxHxxGxxH; in addition to these coordinated histidine residues, serralysin contains a coordinated tyrosine residue that is unique to the astacin-like Zn enzymes. The Zn-endopeptidases containing the histidine motif are structurally similar to one another, containing an N-terminal catalytic domain that belongs to the zincin family, and a C-terminal beta-helix metal-binding domain. These peptidase include the astacin family, snake venom Zn-endopeptidases, the extracellular metalloproteases from Serratia sp., Pseudomonas sp. and Erwinia sp., and the matrixins.

This entry represents the C-terminal domain of serralysins. The serralysin precursor does not possess a signal peptide, instead the C-terminal domain is required for secretion [PMID: 1427098],[PMID: 2211614]. This domain is a 21-strand beta sandwich known as a "parallel beta roll" with the beta strands arranged in a right-handed spiral. There are tandem repeats of a GGXGXDX(L/I/FV)X motif, each of which binds a calcium ion [PMID: 8089845].

Contributing signatures

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