| IED ID | IndEnz0002016348 |
| Enzyme Type ID | protease016348 |
| Protein Name |
Murein tetrapeptide carboxypeptidase EC 3.4.17.13 LD-carboxypeptidase A Muramoyltetrapeptide carboxypeptidase |
| Gene Name | ldcA ycgQ b1192 JW1181 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM |
| Enzyme Length | 304 |
| Uniprot Accession Number | P76008 |
| Absorption | |
| Active Site | ACT_SITE 106; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 200; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 270; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by beta-lactams containing a D-amino acid side chain. {ECO:0000269|PubMed:10428950}. |
| 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; Evidence={ECO:0000269|PubMed:10428950}; |
| DNA Binding | |
| EC Number | 3.4.17.13 |
| Enzyme Function | FUNCTION: Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase. {ECO:0000269|PubMed:10428950, ECO:0000269|PubMed:18535144}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cell wall biogenesis; peptidoglycan recycling. {ECO:0000269|PubMed:10428950}. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (16); Chain (1); Helix (15); Turn (3) |
| Keywords | 3D-structure;Carboxypeptidase;Cell shape;Cell wall biogenesis/degradation;Cytoplasm;Hydrolase;Peptidoglycan synthesis;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10428950}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5Z01; 5Z03; |
| Mapped Pubmed ID | 15690043; 16606699; 24561554; 29601819; 3521529; 3521530; 405375; 780345; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,567 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:48688 |
| Cross Reference Brenda |