ID   Y2153_ENTFA             Reviewed;         568 AA.
AC   Q832R5;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative ABC transporter ATP-binding protein EF_2153;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=EF_2153;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC       energy coupling to the transport system (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE016830; AAO81886.1; -; Genomic_DNA.
DR   RefSeq; NP_815816.1; NC_004668.1.
DR   RefSeq; WP_002380507.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q832R5; -.
DR   SMR; Q832R5; -.
DR   STRING; 226185.EF_2153; -.
DR   PRIDE; Q832R5; -.
DR   EnsemblBacteria; AAO81886; AAO81886; EF_2153.
DR   KEGG; efa:EF2153; -.
DR   PATRIC; fig|226185.45.peg.1375; -.
DR   eggNOG; COG1122; Bacteria.
DR   HOGENOM; CLU_000604_86_7_9; -.
DR   OMA; DPMTRLD; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR022216; ABC_Co_transporter.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12558; DUF3744; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..568
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   EF_2153"
FT                   /id="PRO_0000092009"
FT   DOMAIN          6..247
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          301..535
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   568 AA;  63257 MW;  97FEC94BD7D398FB CRC64;
     MKKPIITFNN FSFQYHSQSE PTLKGIQLTI YEGEKVLIVG PSGSGKSTLA QCINGLIPNI
     YEGEIQGTAT VAGKNIQETS LFDLSFDVGT VLQDTDGQFI GLTVAEDIAF ALENDAVEQA
     EMKKAVQKWS EIVELNQLLQ HRPQDLSGGQ KQRVSMAGVL INQSKILLFD EPLANLDPRA
     GQETMTLIDT IQQETKATVL IIEHRLEDVL CESVDRIIVM NEGTIISDTT PDELLRQDTL
     TQQGIREPLY VTAMKYAGID LTQVSHLDKL AEVSGETVLP KMTQWSVQPS SVSAVKGAEL
     LRLEQVSYQY DRHGEKVLDD FSVTIHHGEM ISIVGKNGAG KSTLSKIICG FITPQSGKIL
     WEGQDFSNYS IKERADKIGY VMQNPNQMIS KKMIFEEVAL GLVLRDVPQA EIEERVTNIL
     HICGLYPFRN WPISALSFGQ KKRVTIASIL VLEPELLILD EPTAGQDFKH YTEMMTFLEE
     LNRLGVTILM ITHDMHLMLE YTTRALVVCD GRLLADATPV AVLTDEKLIQ AASLKETSLF
     TFAKALGLEN PLLFTEKFVA YDREVRFG