| IED ID | IndEnz0002009958 |
| Enzyme Type ID | protease009958 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase D,D-carboxypeptidase D-Ala-D-Ala carboxypeptidase EC 3.4.17.- |
| Gene Name | vanYB EF_2297 |
| Organism | Enterococcus faecalis (strain ATCC 700802 / V583) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecalis (Streptococcus faecalis) Enterococcus faecalis (strain ATCC 700802 / V583) |
| Enzyme Sequence | MEKSNYHSNVNHHKRHMKQSGEKRAFLWAFIISFTVCTLFLGWRLVSVLEATQLPPIPATHTGSGTGVAENPEENTLATAKEQGDEQEWSLILVNRQNPIPAQYDVELEQLSNGERIDIRISPYLQDLFDAARADGVYPIVASGYRTTEKQQEIMDEKVAEYKAKGYTSAQAKAEAETWVAVPGTSEHQLGLAVDINADGIHSTGNEVYRWLDENSYRFGFIRRYPPDKTEITGVSNEPWHYRYVGIEAATKIYHQGLCLEEYLNTEK |
| Enzyme Length | 268 |
| Uniprot Accession Number | Q47746 |
| Absorption | |
| Active Site | ACT_SITE 238; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:30016658 |
| Activity Regulation | ACTIVITY REGULATION: Carboxypeptidase activity is insensitive to beta-lactams since it is not affected by penicillin G or ampicillin and is inhibited only by very high concentrations of cefalotin and cefoxitin. {ECO:0000269|PubMed:8631706}. |
| Binding Site | BINDING 151; /note=Substrate; /evidence=ECO:0000269|PubMed:30016658; BINDING 186; /note=Substrate; /evidence=ECO:0000269|PubMed:30016658 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Carboxypeptidase that cleaves the C-terminal D-alanine residue from the peptidoglycan-derived pentapeptide L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala in vitro. Therefore, should contribute in vivo to the hydrolysis of the D-alanyl-D-alanine-containing peptidoglycan precursors. May increase the level of glycopeptide antibiotics resistance by decreasing the availability of D-Ala-D-Ala termini from the cell surface, which constitute the antibiotic target residues. {ECO:0000269|PubMed:8631706}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Binding site (2); Chain (1); Helix (12); Metal binding (3); Region (1); Transmembrane (1); Turn (1) |
| Keywords | 3D-structure;Antibiotic resistance;Carboxypeptidase;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Metal-binding;Peptidoglycan synthesis;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By vancomycin, mediated by VanS/VanR. Part of the VanB-type operon associated to vancomycin resistance in E.faecalis V583. {ECO:0000269|PubMed:8631706}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8631706}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 5HNM; 5ZHF; 5ZHW; 6A6A; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,382 |
| Kinetics | |
| Metal Binding | METAL 188; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000269|PubMed:30016658, ECO:0007744|PDB:5HNM"; METAL 195; /note="Zinc"; /evidence="ECO:0000269|PubMed:30016658, ECO:0007744|PDB:5HNM"; METAL 241; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000269|PubMed:30016658, ECO:0007744|PDB:5HNM" |
| Rhea ID | |
| Cross Reference Brenda |