ID   FRUK_BIFLO              Reviewed;         513 AA.
AC   Q8G847;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Fructose import ATP-binding protein FruK {ECO:0000305};
DE            EC=7.5.2.- {ECO:0000269|PubMed:22102285};
GN   Name=fruK {ECO:0000303|PubMed:22102285};
GN   OrderedLocusNames=BL0034 {ECO:0000312|EMBL:AAN23901.1};
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH FRUF AND FRUG.
RC   STRAIN=NCC 2705;
RX   PubMed=22102285; DOI=10.1074/jbc.m111.266213;
RA   Wei X., Guo Y., Shao C., Sun Z., Zhurina D., Liu D., Liu W., Zou D.,
RA   Jiang Z., Wang X., Zhao J., Shang W., Li X., Liao X., Huang L.,
RA   Riedel C.U., Yuan J.;
RT   "Fructose uptake in Bifidobacterium longum NCC2705 is mediated by an ATP-
RT   binding cassette transporter.";
RL   J. Biol. Chem. 287:357-367(2012).
CC   -!- FUNCTION: Part of the high-affinity ABC transporter complex FruEKFG
CC       involved in fructose uptake. Can also transport ribose and xylose, with
CC       lower affinity. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000269|PubMed:22102285}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-fructose(out) + H2O = ADP + D-fructose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:60180, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:22102285};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60181;
CC         Evidence={ECO:0000269|PubMed:22102285};
CC   -!- SUBUNIT: The complex is composed of an ATP-binding protein (FruK), two
CC       transmembrane proteins (FruF and FruG) and a solute-binding protein
CC       (FruE). {ECO:0000269|PubMed:22102285}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE014295; AAN23901.1; -; Genomic_DNA.
DR   RefSeq; NP_695265.1; NC_004307.2.
DR   RefSeq; WP_007053223.1; NC_004307.2.
DR   AlphaFoldDB; Q8G847; -.
DR   SMR; Q8G847; -.
DR   STRING; 206672.BL0034; -.
DR   TCDB; 3.A.1.2.23; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; AAN23901; AAN23901; BL0034.
DR   GeneID; 66505652; -.
DR   KEGG; blo:BL0034; -.
DR   PATRIC; fig|206672.9.peg.36; -.
DR   HOGENOM; CLU_000604_92_3_11; -.
DR   OMA; GFGFCPE; -.
DR   PhylomeDB; Q8G847; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..513
FT                   /note="Fructose import ATP-binding protein FruK"
FT                   /id="PRO_0000439269"
FT   DOMAIN          8..244
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          262..505
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   513 AA;  55835 MW;  F47F2AFFB6798AB9 CRC64;
     MTDKNPIVVM KGITIEFPGV KALDGVDLTL YPGEVHALMG ENGAGKSTMI KALTGVYKIN
     AGSIMVDGKP QQFNGTLDAQ NAGIATVYQE VNLCTNLSVG ENVMLGHEKR GPFGIDWKKT
     HEAAKKYLAQ MGLESIDPHT PLSSISIAMQ QLVAIARAMV INAKVLILDE PTSSLDANEV
     RDLFAIMRKV RDSGVAILFV SHFLDQIYEI TDRLTILRNG QFIKEVMTKD TPRDELIGMM
     IGKSAAELSQ IGAKKARREI TPGEKPIVDV KGLGKKGTIN PVDVDIYKGE VVGFAGLLGS
     GRTELGRLLY GADKPDSGTY TLNGKKVNIS DPYTALKNKI AYSTENRRDE GIIGDLTVRQ
     NILIALQATR GMFKPIPKKE ADAIVDKYMK ELNVRPADPD RPVKNLSGGN QQKVLIGRWL
     ATHPELLILD EPTRGIDIGA KAEIQQVVLD LASQGMGVVF ISSELEEVVR LSDDIEVLKD
     RHKIAEIEND DTVSQATIVE TIANTNVNTG KEA