ID   VANC_ENTGA              Reviewed;         343 AA.
AC   P29753;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Vancomycin C-type resistance protein VanC;
DE            EC=6.3.2.-;
DE   AltName: Full=VanC ligase;
GN   Name=vanC;
OS   Enterococcus gallinarum.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BM4174;
RX   PubMed=1551598; DOI=10.1016/0378-1119(92)90302-6;
RA   Dutka-Malen S., Molinas C., Arthur M., Courvalin P.;
RT   "Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-
RT   alanine:D-alanine ligase-related protein necessary for vancomycin
RT   resistance.";
RL   Gene 112:53-58(1992).
CC   -!- FUNCTION: Required for low-level resistance to the glycopeptide
CC       antibiotic vancomycin. Probable D-alanine--D-alanine ligase of altered
CC       specificity. It may synthesize a dipeptide or a depsipeptide which is
CC       incorporated into peptidoglycan precursors and not recognized by
CC       vancomycin.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side.
CC   -!- INDUCTION: By vancomycin.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AF162694; AAA24786.1; -; Genomic_DNA.
DR   PIR; JN0249; JN0249.
DR   RefSeq; WP_029487031.1; NZ_QYOK01000008.1.
DR   AlphaFoldDB; P29753; -.
DR   SMR; P29753; -.
DR   KEGG; ag:AAA24786; -.
DR   BioCyc; MetaCyc:MON-15483; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   2: Evidence at transcript level;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Ligase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN           1..343
FT                   /note="Vancomycin C-type resistance protein VanC"
FT                   /id="PRO_0000177919"
FT   DOMAIN          134..336
FT                   /note="ATP-grasp"
FT   BINDING         164..219
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  37547 MW;  FA23D5F5722E2602 CRC64;
     MKKIAVLFGG NSPEYSVSLT SAASVIQAID PLKYEVMTIG IAPTMDWYWY QGNLANVRND
     TWLEDHKNCH QLTFSSQGFI LGEKRIVPDV LFPVLHGKYG EDGCIQGLLE LMNLPYVGCH
     VAASALCMNK WLLHQLADTM GIASAPTLLL SRYENDPATI DRFIQDHGFP IFIKPNEAGS
     SKGITKVTDK TALQSALTTA FAYGSTVLIQ KAIAGIEIGC GILGNEQLTI GACDAISLVD
     GFFDFEEKYQ LISATITVPA PLPLALESQI KEQAQLLYRN LGLTGLARID FFVTNQGAIY
     LNEINTMPGF TGHSRYPAMM AEVGLSYEIL VEQLIALAEE DKR