Detail Information for IndEnz0002012894
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