| IED ID | IndEnz0002016113 |
| Enzyme Type ID | protease016113 |
| Protein Name |
Murein peptide amidase A EC 3.4.17.- Gamma-D-Glu-Dap amidase Zinc metallocarboxypeptidase MpaA |
| Gene Name | mpaA Z2448 ECs1905 |
| Organism | Escherichia coli O157:H7 |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7 |
| Enzyme Sequence | MTVTRPRAERGAFPPGTEHYGRSLLGAPLIWFPAPAASRESGLILAGTHGDENSSVVTLSCALRTLTPSLRRHHVVLCVNPDGCQLGLRANANGVDLNRNFPAANWKEGETVYRWNSAAEERDVVLLTGDKPGSEPETQALCQLIHRIQPAWVVSFHDPLACIEDPRHSELGEWLAQAFELPLVTSVGYETPGSFGSWCADLNLHCITAEFPPISSDEASEKYLFAMANLLRWHPKDAIRPS |
| Enzyme Length | 242 |
| Uniprot Accession Number | P0ACV7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate = L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate; Xref=Rhea:RHEA:28398, ChEBI:CHEBI:15377, ChEBI:CHEBI:57791, ChEBI:CHEBI:61395, ChEBI:CHEBI:61401; Evidence={ECO:0000255|HAMAP-Rule:MF_02211}; |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap. {ECO:0000255|HAMAP-Rule:MF_02211}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall degradation; peptidoglycan degradation. {ECO:0000255|HAMAP-Rule:MF_02211}. |
| nucleotide Binding | |
| Features | Beta strand (10); Chain (1); Erroneous initiation (2); Helix (10); Metal binding (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell wall biogenesis/degradation;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02211}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5HXD; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 26,558 |
| Kinetics | |
| Metal Binding | METAL 49; /note=Zinc; via pros nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_02211; METAL 52; /note=Zinc; /evidence=ECO:0000255|HAMAP-Rule:MF_02211; METAL 157; /note=Zinc; via pros nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_02211 |
| Rhea ID | RHEA:28398 |
| Cross Reference Brenda |