Family M73


Summary Holotypes Alignment Tree Genomes Literature

Summary for family M73

Family type peptidaseM73.001 - camelysin (Bacillus cereus), MEROPS Accession MER0031615 (peptidase unit: 28-197)
Content of familyPeptidase family M73 contains metallo-endopeptidases.
History Identifier created: MEROPS 6.7 (29 June 2004)
Peptidase family M73 includes a cell-surface endopeptidase from Bacillus cereus known as camelysin (M73.001).
Catalytic typeMetallo
Active siteActive site residues and metal ligands have not been determined. Completely conserved potential metal ligands are Asp31, Asp63, Asn73, Asp101, Gln173 and Gln177, though not all members of the family are known to be active peptidases. No histidine is conserved in the family. The only other family of metallopeptidases in which none of the metal ligands are histidine is family M63. The metal content has been determined as one zinc ion per molecule (Grass et al., 2004).
Activities and specificitiesCamelysin has been shown to cleave proteins such as caseins, actin and collagen type I. Specificity has been determined to be cleavage of bonds with an aliphatic or hydrophilic residue in P1" (Fricke et al., 2001).
InhibitorsCamelysin is inhibited by the chelating agents EDTA and 1,10-phenanthroline at millimolar concentrations. Inhibition was also seen with 10 mM diethylpyrocarbonate, which modifies histidine residues (Fricke et al., 2001), even though a histidine residue is not conserved in the family.
Molecular structureNo tertiary structure has been determined for any member of the family. Camelysin is predicted to have an N-terminal signal peptide, and is strongly bound to the cell surface (Grass et al., 2004).
Distribution of family Bacteria details  
Archaea details  
Protozoa -  
Fungi -  
Plants -  
Animals -  
Viruses -  
Biological functions
Pharmaceutical and biotech relevanceBacillus cereus is a causative agent of food poisoning and is implicated in secondary infections in hospitals (nosocomial diseases). Camelysin may have a role in bacterial invasion, because it is collagenolytic, and in penetration of fibrin clots, because it can activate plasminogen (Fricke et al., 2001).
Statistics for family M73Sequences:193
Identifiers with PDB entries:0
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Peptidases and Homologues MEROPS ID Structure
spore coat-associated protein N (Bacillus subtilis)M73.A01-
family M73 unassigned peptidasesunassigned-