ID   VANTE_ENTFL             Reviewed;         702 AA.
AC   Q93A44;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Amino-acid racemase;
DE            EC=5.1.1.-;
DE   AltName: Full=Vancomycin E-type resistance protein VanT;
GN   Name=vanTE;
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=N00-410;
RX   PubMed=12019119; DOI=10.1128/aac.46.6.1977-1979.2002;
RA   Boyd D.A., Cabral T., Van Caeseele P., Wylie J., Mulvey M.R.;
RT   "Molecular characterization of the vanE gene cluster in vancomycin-
RT   resistant Enterococcus faecalis N00-410 isolated in Canada.";
RL   Antimicrob. Agents Chemother. 46:1977-1979(2002).
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; FJ872411; AAL27444.1; -; Genomic_DNA.
DR   RefSeq; WP_063856753.1; NG_048456.1.
DR   AlphaFoldDB; Q93A44; -.
DR   SMR; Q93A44; -.
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..702
FT                   /note="Amino-acid racemase"
FT                   /id="PRO_0000114608"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..702
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          337..702
FT                   /note="Racemase"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        601
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         650
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         375
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   702 AA;  79440 MW;  AEC852BF1B3D3056 CRC64;
     MKHRANGIDL FRIFAATMVV AIHTFPFQSI APFLDEVITL TVFRVAVPFF FMITGYFLLG
     RLSLNFSYNN NQRVKKYLYK IGMIYLYSIL LYFPLSLLNG TISLKMNILL LLKVFIFDGT
     FYHLWYFPAS IIGTILVTLL LRSIGFKLTV AFSTCLYLVG LGGDSWYGIT NQVPLLNKLY
     TFIFSWSDYT RSGVFFTPVF LCLGIFAYRV SKKLTASKIL NLLFYVFIIG MTFESIFLHR
     FTNVKHDSMY LLLPSCALIL FLMLLNWQPK LKVKESADLT LLVYILHPLV IVIVHSISKY
     IPILKNSLLN FLLVVVCSFI LAQLLLNLKR KLRVSKQKIP FERASKEISA SAIHHNINEI
     RKIIPKNTNI MGVVKANAYG CGMVEVAYEL EKIGISFFCV ATIEEAIALR KSGNQGDILI
     LGYTHPNRIN DIKKYNLIQS IVSEEHGKVL NLKKIPIRCH LQVDTGMHRL GVTPNVTIIQ
     QMYLFSNLKI EGIYSHLGSS DSLEQESIAR TNTQIFLFNN ILSDLEQMGI SYGYTHIQSS
     YGILNYPELS FDFVRIGILC YGFLSDYNSP TKIPIDLQPI VKVKASLITE RIVEAGEYVG
     YGLGAKVEKR TRIGVVSIGY ADGIPRALSN AKLTLEFKGQ SIKQIGNICM DMMLVDLSEV
     EDISLNDELI VLPNISKIAD EEQTITNELL SRLGSRLGTE LN