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  Domain Name: M14_MpaA_like
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins. Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 12
Total Disease Mutations Found: 3
This domain occurred 10 times on human genes (11 proteins).



  CARBOXYPEPTIDASE N DEFICIENCY
  EPILEPSY, FAMILIAL TEMPORAL LOBE, 5
  FEBRILE SEIZURES, FAMILIAL, 11


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
Zn binding site
putative active site














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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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