InterPro domain: IPR011049

Serralysin is a bacterial Zn-endopeptidase that acts as a virulence factor to cause tissue damage and anaphylactic response [ 1 ]. 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 [ 2 , 3 ]. 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 [ 4 ].

1. Mechanistic studies of the astacin-like Serratia metalloendopeptidase serralysin: highly active (>2000%) Co(II) and Cu(II) derivatives for further corroboration of a "metallotriad" mechanism. J. Biol. Inorg. Chem. 7, 600-10
2. Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways. Gene 121, 47-54
3. Protein secretion in gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin. J. Biol. Chem. 265, 17118-25
4. Crystal structure of the 50 kDa metallo protease from Serratia marcescens. J. Mol. Biol. 242, 244-51