| IED ID | IndEnz0002009596 |
| Enzyme Type ID | protease009596 |
| Protein Name |
Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase EC 3.4.-.- EC 3.4.17.13 Lipoprotein Spr Murein hydrolase MepS |
| Gene Name | mepS spr Z3434 ECs3067 |
| Organism | Escherichia coli O157:H7 |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O157:H7 |
| Enzyme Sequence | MVKSQPILRYILRGIPAIAVAVLLSACSANNTAKNMHPETRAVGSETSSLQASQDEFENLVRNVDVKSRIMDQYADWKGVRYRLGGSTKKGIDCSGFVQRTFREQFGLELPRSTYEQQEMGKSVSRSNLRTGDLVLFRAGSTGRHVGIYIGNNQFVHASTSSGVIISSMNEPYWKKRYNEARRVLSRS |
| Enzyme Length | 188 |
| Uniprot Accession Number | P0AFV6 |
| Absorption | |
| Active Site | ACT_SITE 94; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 145; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 157; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl; Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13; |
| DNA Binding | |
| EC Number | 3.4.-.-; 3.4.17.13 |
| Enzyme Function | FUNCTION: A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Lipidation (2); Signal peptide (1) |
| Keywords | Cell outer membrane;Hydrolase;Lipoprotein;Membrane;Palmitate;Protease;Reference proteome;Signal;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,040 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:48688 |
| Cross Reference Brenda |