| IED ID | IndEnz0002008084 |
| Enzyme Type ID | protease008084 |
| Protein Name |
Penicillin-insensitive murein endopeptidase EC 3.4.24.- D-alanyl-D-alanine-endopeptidase DD-endopeptidase |
| Gene Name | mepA b2328 JW2325 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQSWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI |
| Enzyme Length | 274 |
| Uniprot Accession Number | P0C0T5 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Zn(2+) at 10 mM and by metal chelating agents EDTA and 1,10-phenanthroline. {ECO:0000269|PubMed:15292190}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. {ECO:0000269|PubMed:15292190}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-8. {ECO:0000269|PubMed:15292190}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (11); Chain (1); Disulfide bond (3); Helix (9); Metal binding (6); Mutagenesis (4); Region (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Periplasm;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:15292190}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:2187143 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1TZP; 1U10; |
| Mapped Pubmed ID | 14687573; 15044722; 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 30,137 |
| Kinetics | |
| Metal Binding | METAL 110; /note=Zinc 1; /evidence=ECO:0000269|PubMed:15292190; METAL 113; /note=Zinc 1; /evidence=ECO:0000269|PubMed:15292190; METAL 120; /note=Zinc 1; /evidence=ECO:0000269|PubMed:15292190; METAL 147; /note=Zinc 2; /evidence=ECO:0000269|PubMed:15292190; METAL 150; /note=Zinc 2; /evidence=ECO:0000269|PubMed:15292190; METAL 211; /note=Zinc 1; /evidence=ECO:0000269|PubMed:15292190 |
| Rhea ID | |
| Cross Reference Brenda |