IED ID | IndEnz0002012894 |
Enzyme Type ID | protease012894 |
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 yeiV b2175 JW2163 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MVKSQPILRYILRGIPAIAVAVLLSACSANNTAKNMHPETRAVGSETSSLQASQDEFENLVRNVDVKSRIMDQYADWKGVRYRLGGSTKKGIDCSGFVQRTFREQFGLELPRSTYEQQEMGKSVSRSNLRTGDLVLFRAGSTGRHVGIYIGNNQFVHASTSSGVIISSMNEPYWKKRYNEARRVLSRS |
Enzyme Length | 188 |
Uniprot Accession Number | P0AFV4 |
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. Partially suppresses a prc disruption mutant. {ECO:0000269|PubMed:23062283, ECO:0000269|PubMed:9158724}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. |
nucleotide Binding | |
Features | Active site (3); Beta strand (6); Chain (1); Domain (1); Helix (6); Lipidation (2); Mutagenesis (1); Signal peptide (1); Turn (2) |
Keywords | 3D-structure;Cell outer membrane;Cell wall biogenesis/degradation;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 | NMR spectroscopy (1) |
Cross Reference PDB | 2K1G; |
Mapped Pubmed ID | 16606699; |
Motif | |
Gene Encoded By | |
Mass | 21,040 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:48688 |
Cross Reference Brenda |