Summary for clan MO
| Clan type peptidase | M23.013 - LytM glycyl-glycine endopeptidase (Staphylococcus aureus) (Staphylococcus aureus), MEROPS Accession MER0003906 (peptidase unit: 188-321); PDB accession 1QWY |
| History | MEROPS 6.6 (27 March 2004) |
| Description | Water nucleophile; water bound by single zinc ion ligated to two His and Asp (within the motifs HXXXD and HXH) |
| Contents of clan | Clan MO contains only family M23, the peptidases in which are endopeptidases. |
| Evidence | For 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 activity | The peptidase in the family has a preference for cleavage of Gly bonds. |
| Protein fold | The 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 families | The 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.) |
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Other databases
| SCOP | 51261 |
Families
| M23 |
beta-lytic metallopeptidase (Achromobacter lyticus) |
Yes |
Distribution of clan MO among Kingdoms of Organisms
