AC MF_01623; DC Protein; auto TR HAMAP; MF_01623; -; 1; level=0 XX Names: MepA XX ID MEPA DE RecName: Full=Penicillin-insensitive murein endopeptidase; DE EC=3.4.24.-; DE AltName: Full=D-alanyl-D-alanine-endopeptidase; DE Short=DD-endopeptidase; DE Flags: Precursor; GN Name=mepA; XX CC -!- FUNCTION: Murein endopeptidase that cleaves the D-alanyl-meso-2,6- CC diamino-pimelyl amide bond that connects peptidoglycan strands. Likely CC plays a role in the removal of murein from the sacculus. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the CC active site. Zn(2+) ion 2 is bound at the dimer interface by residues CC from both subunits.; CC -!- SUBUNIT: Dimer. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the peptidase M74 family. XX DR Pfam; PF03411; Peptidase_M74; 1; trigger=no DR PIRSF; PIRSF018455; MepA; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX case or or KW Disulfide bond end case KW Hydrolase KW Metal-binding KW Metalloprotease KW Periplasm KW Protease KW Signal KW Zinc XX GO GO:0004222; F:metalloendopeptidase activity GO GO:0000270; P:peptidoglycan metabolic process GO GO:0042597; C:periplasmic space XX FT From: MEPA_ECOLI (P0C0T5) FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: D FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H FT BINDING 211 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT DISULFID 44..265 FT Condition: C-x*-C FT DISULFID 187..235 FT Condition: C-x*-C FT DISULFID 216..223 FT Condition: C-x*-C XX Size: 274-281; Related: None; Template: P0C0T5; Scope: Bacteria; Enterobacterales Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.19 2022/11/19 //