ID   VANTG_ENTFL             Reviewed;         711 AA.
AC   Q9KHL7;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Amino-acid racemase;
DE            EC=5.1.1.-;
DE   AltName: Full=Vancomycin G-type resistance protein VanT;
GN   Name=vanTG;
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCH9;
RX   PubMed=11036060; DOI=10.1128/aac.44.11.3224-3228.2000;
RA   McKessar S.J., Berry A.M., Bell J.M., Turnidge J.D., Paton J.C.;
RT   "Genetic characterization of vanG, a novel vancomycin resistance locus of
RT   Enterococcus faecalis.";
RL   Antimicrob. Agents Chemother. 44:3224-3228(2000).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acyltransferase 3
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the alanine racemase
CC       family. {ECO:0000305}.
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DR   EMBL; AF253562; AAF71283.1; -; Genomic_DNA.
DR   RefSeq; WP_063856752.1; NG_048455.1.
DR   AlphaFoldDB; Q9KHL7; -.
DR   SMR; Q9KHL7; -.
DR   PRIDE; Q9KHL7; -.
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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011248; Serine/alanine_racemase.
DR   Pfam; PF01757; Acyl_transf_3; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF036464; Ser_ala_racem; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Isomerase; Membrane;
KW   Pyridoxal phosphate; Transmembrane; Transmembrane helix.
FT   CHAIN           1..711
FT                   /note="Amino-acid racemase"
FT                   /id="PRO_0000114607"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..37
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..711
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          336..711
FT                   /note="Racemase"
FT   ACT_SITE        376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        602
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         651
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         376
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   711 AA;  80163 MW;  2A710DAEE2578404 CRC64;
     MTKNESYSGI DYFRFIAALL IVAIHTSPLF SFSETGNFIF TRIVAPVAVP FFFMTSGFFL
     ISRYTCNAEK LGAFIKKTTL IYGVAILLYI PINVYNGYFK MDNLLPNIIK DIVFDGTLYH
     LWYLPASIIG AAIAWYLVKK VHYRKAFLIA SILYIIGLFG DSYYGIVKSV SCLNVFYNLI
     FQLTDYTRNG IFFAPIFFVL GGYISDSPNR YRKKNYIRIY SLFCLMFGKT LTLQHFDIQK
     HDSMYVLLLP SVWCLFNLLL HFRGKRRTGL RTISLDQLYH SSVYDCCNTI VCAELLHLQS
     LLVENSLVHY IAVCFASVVL AVVITALLSS LKPKKAKHTA DTDRAYLEIN LNNLEHNVNT
     LQKAMSPKCE LMAVVKAEAY GHGMYEVTTY FEPIGVFYLA VATIDEGIRL RKYGIFSEIL
     ILGYTSPSRA KELCKFELTQ TLIDYRYLLL LNKQGYDIKA HIKIDTGMHR LGFSTEDKDK
     ILAAFFLKHI KVAGIFTHLC AADSLEEKEV AFTNKPIGSF YKVLDWPKSS GLNIPKVNIQ
     TSYGLWNIQS WNVIYQSGVA LYGVLRSTND KTKLETDLRA CSFLKAKVVL IRKIKQGGSV
     GYSRAFTATR DSLIAILPIG YADGFPRNLS CGNSYVLIGG RQAPIVGKIC MDQLAVDVTD
     IPNVKTGSIA TLIGKDGKEE ITAPMVAESA ESITNELLSR MEHRLNIIRR A