| IED ID | IndEnz0002013692 |
| Enzyme Type ID | protease013692 |
| Protein Name |
D-alanyl-D-alanine carboxypeptidase D,D-carboxypeptidase D-Ala-D-Ala carboxypeptidase DD-carboxypeptidase EC 3.4.17.- |
| Gene Name | vanY |
| Organism | Enterococcus faecium (Streptococcus faecium) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecium (Streptococcus faecium) |
| Enzyme Sequence | MKKLFFLLLLLFLIYLGYDYVNEALFSQEKVEFQNYDQNPKEHLENSGTSENTQEKTITEEQVYQGNLLLINSKYPVRQESVKSDIVNLSKHDELINGYGLLDSNIYMSKEIAQKFSEMVNDAVKGGVSHFIINSGYRDFDEQSVLYQEMGAEYALPAGYSEHNSGLSLDVGSSLTKMERAPEGKWIEENAWKYGFILRYPEDKTELTGIQYEPWHIRYVGLPHSAIMKEKNFVLEEYMDYLKEEKTISVSVNGEKYEIFYYPVTKNTTIHVPTNLRYEISGNNIDGVIVTVFPGSTHTNSRR |
| Enzyme Length | 303 |
| Uniprot Accession Number | P37711 |
| Absorption | |
| Active Site | ACT_SITE 213; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q47746 |
| Activity Regulation | ACTIVITY REGULATION: The DD-carboxypeptidase activity is not inhibited by beta-lactam antibiotics. {ECO:0000269|PubMed:1510448}. |
| Binding Site | BINDING 161; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q47746 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide (UDP-MurNAc-L-Ala-D-Glu-mDAP-D-Ala-D-Ala) (PubMed:1510448). However the physiological substrate likely contains L-Lys instead of mDAP at the third position of the pentapeptide (Probable). Also releases the C-terminal D-lactate from UDP-MurNAc-L-Ala-D-Glu-mDAP-D-Ala-D-lactate, a depsipeptide produced by the vancomycin resistance protein VanA. Therefore, VanY should contribute in vivo to the hydrolysis of both the D-alanyl-D-alanine- and the depsipeptide-containing peptidoglycan precursors (PubMed:1510448). Is not necessary for vancomycin resistance of E.faecium BM4147 (PubMed:1398115). Does not display transpeptidase or beta-lactamase activities (PubMed:1510448). {ECO:0000269|PubMed:1398115, ECO:0000269|PubMed:1510448, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Metal binding (3); Region (2); Transmembrane (1) |
| Keywords | Carboxypeptidase;Cell membrane;Cell shape;Cell wall biogenesis/degradation;Hydrolase;Membrane;Metal-binding;Peptidoglycan synthesis;Plasmid;Protease;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By vancomycin. Part of the van gene cluster of pIP816, the plasmid that confers high-level resistance to vancomycin in E.faecium BM4147. {ECO:0000269|PubMed:1398115}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1510448}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pIP816 |
| Mass | 34,980 |
| Kinetics | |
| Metal Binding | METAL 163; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q47746; METAL 170; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q47746; METAL 216; /note=Zinc; via pros nitrogen; /evidence=ECO:0000250|UniProtKB:Q47746 |
| Rhea ID | |
| Cross Reference Brenda |