Peptidase M35 domain of peptidyl-Lys metalloendopeptidases
This family M35 Zn2+-metallopeptidase extracellular domain is mostly found in proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20), including some well-characterized domains in Aeromonas salmonicida subsp. Achromogenes (AsaP1) and Grifola frondosa (GfMEP). These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response. Members of this family contain a unique zinc-binding motif (the aspzincin motif), defined by the HExxH + D motif where an aspartic acid is the third zinc ligand and is found in a GTXDXXYG or similar motif C-terminal to the His zinc ligands.