VANY_ENTFC
ID VANY_ENTFC Reviewed; 303 AA.
AC P37711;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000305};
DE Short=D,D-carboxypeptidase {ECO:0000303|PubMed:1398115};
DE Short=D-Ala-D-Ala carboxypeptidase {ECO:0000305};
DE Short=DD-carboxypeptidase {ECO:0000303|PubMed:1510448};
DE EC=3.4.17.- {ECO:0000305};
GN Name=vanY {ECO:0000303|PubMed:1398115};
OS Enterococcus faecium (Streptococcus faecium).
OG Plasmid pIP816.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1352;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=BM4147;
RX PubMed=1398115; DOI=10.1016/0378-1119(92)90017-j;
RA Arthur M., Molinas C., Courvalin P.;
RT "Sequence of the vanY gene required for production of a vancomycin-
RT inducible D,D-carboxypeptidase in Enterococcus faecium BM4147.";
RL Gene 120:111-114(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BM4147; TRANSPOSON=Tn1546;
RX PubMed=8380148; DOI=10.1128/jb.175.1.117-127.1993;
RA Arthur M., Molinas C., Depardieu F., Courvalin P.;
RT "Characterization of Tn1546, a Tn3-related transposon conferring
RT glycopeptide resistance by synthesis of depsipeptide peptidoglycan
RT precursors in Enterococcus faecium BM4147.";
RL J. Bacteriol. 175:117-127(1993).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BM4147;
RX PubMed=1510448; DOI=10.1128/aac.36.7.1514;
RA Wright G.D., Molinas C., Arthur M., Courvalin P., Walsh C.T.;
RT "Characterization of vanY, a DD-carboxypeptidase from vancomycin-resistant
RT Enterococcus faecium BM4147.";
RL Antimicrob. Agents Chemother. 36:1514-1518(1992).
CC -!- FUNCTION: Cleaves the C-terminal D-alanine residue of UDP-muramyl-
CC pentapeptide (UDP-MurNAc-L-Ala-D-Glu-mDAP-D-Ala-D-Ala)
CC (PubMed:1510448). However the physiological substrate likely contains
CC L-Lys instead of mDAP at the third position of the pentapeptide
CC (Probable). Also releases the C-terminal D-lactate from UDP-MurNAc-L-
CC Ala-D-Glu-mDAP-D-Ala-D-lactate, a depsipeptide produced by the
CC vancomycin resistance protein VanA. Therefore, VanY should contribute
CC in vivo to the hydrolysis of both the D-alanyl-D-alanine- and the
CC depsipeptide-containing peptidoglycan precursors (PubMed:1510448). Is
CC not necessary for vancomycin resistance of E.faecium BM4147
CC (PubMed:1398115). Does not display transpeptidase or beta-lactamase
CC activities (PubMed:1510448). {ECO:0000269|PubMed:1398115,
CC ECO:0000269|PubMed:1510448, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q47746};
CC -!- ACTIVITY REGULATION: The DD-carboxypeptidase activity is not inhibited
CC by beta-lactam antibiotics. {ECO:0000269|PubMed:1510448}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1510448};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: By vancomycin. Part of the van gene cluster of pIP816, the
CC plasmid that confers high-level resistance to vancomycin in E.faecium
CC BM4147. {ECO:0000269|PubMed:1398115}.
CC -!- SIMILARITY: Belongs to the peptidase M15B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M97297; AAA65958.1; -; Genomic_DNA.
DR EMBL; M90647; AAA98147.1; -; Genomic_DNA.
DR PIR; JC1427; JC1427.
DR RefSeq; WP_001812592.1; NZ_WSZC01000082.1.
DR RefSeq; YP_001019033.1; NC_008821.1.
DR RefSeq; YP_001974794.1; NC_010980.1.
DR RefSeq; YP_002128401.1; NC_011140.1.
DR RefSeq; YP_976075.1; NC_008768.1.
DR AlphaFoldDB; P37711; -.
DR SMR; P37711; -.
DR MEROPS; M15.010; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR003709; Pept_M15B.
DR Pfam; PF02557; VanY; 1.
DR SUPFAM; SSF55166; SSF55166; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Membrane; Metal-binding;
KW Peptidoglycan synthesis; Plasmid; Protease; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..303
FT /note="D-alanyl-D-alanine carboxypeptidase"
FT /id="PRO_0000195472"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q47746"
FT BINDING 154..156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q47746"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q47746"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q47746"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q47746"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q47746"
SQ SEQUENCE 303 AA; 34980 MW; 21D6B088C14DB565 CRC64;
MKKLFFLLLL LFLIYLGYDY VNEALFSQEK VEFQNYDQNP KEHLENSGTS ENTQEKTITE
EQVYQGNLLL INSKYPVRQE SVKSDIVNLS KHDELINGYG LLDSNIYMSK EIAQKFSEMV
NDAVKGGVSH FIINSGYRDF DEQSVLYQEM GAEYALPAGY SEHNSGLSLD VGSSLTKMER
APEGKWIEEN AWKYGFILRY PEDKTELTGI QYEPWHIRYV GLPHSAIMKE KNFVLEEYMD
YLKEEKTISV SVNGEKYEIF YYPVTKNTTI HVPTNLRYEI SGNNIDGVIV TVFPGSTHTN
SRR
