Summary for clan MO

Summary Alignment Structure Literature
Clan type peptidaseM23.013 - LytM glycyl-glycine endopeptidase (Staphylococcus aureus) (Staphylococcus aureus), MEROPS Accession MER0003906 (peptidase unit: 216-321); PDB accession 1QWY
HistoryMEROPS 6.6 (27 March 2004)
DescriptionWater nucleophile; water bound by single zinc ion ligated to two His and Asp (within the motifs HXXXD and HXH)
Contents of clanClan MO contains only family M23, the peptidases in which are endopeptidases.
EvidenceFor members of this family zinc ligands occur in the motifs HXXXXD and HXH which is unlike that in any other family. The first His (sometime replaced by Glu) in the second motif is the active residue (Odintsov et al., 2004) (See the family M23 Alignment).
Catalytic mechanism(See family M23.)
Peptidase activityThe peptidase in the family has a preference for cleavage of Glybonds.
Protein foldThe tertiary structure of autolysin LytM from Staphylococcus aureus has been determined (Firczuk et al., 2005). Peptidases in clan MO are all beta proteins containing two, stacked half beta-barrels. The active site is at the end of the larger, C-terminal barrel.
Homologous non-peptidase familiesThe IIa domain of glucose permease from Bacillus subtilis and the glucose-specific factor III from Escherichia coli have similar structures (SCOP sunid 51261).
Activation mechanism(See family M23.)
Other databases SCOP51261


Family Family Type Peptidase Structure
M23 beta-lytic metallopeptidase (Achromobacter lyticus) Yes

Distribution of clan MO among Kingdoms of Organisms