FRUG_BIFLO
ID FRUG_BIFLO Reviewed; 340 AA.
AC Q8G845;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Fructose import permease protein FruG {ECO:0000305};
GN Name=fruG {ECO:0000303|PubMed:22102285};
GN OrderedLocusNames=BL0036 {ECO:0000312|EMBL:AAN23903.1};
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, SUBUNIT, AND INTERACTION WITH FRUK AND FRUE.
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 the translocation of the
CC substrate across the membrane. {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}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; AE014295; AAN23903.1; -; Genomic_DNA.
DR RefSeq; NP_695267.1; NC_004307.2.
DR RefSeq; WP_007053225.1; NC_004307.2.
DR AlphaFoldDB; Q8G845; -.
DR STRING; 206672.BL0036; -.
DR TCDB; 3.A.1.2.23; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAN23903; AAN23903; BL0036.
DR GeneID; 66505650; -.
DR KEGG; blo:BL0036; -.
DR PATRIC; fig|206672.9.peg.38; -.
DR HOGENOM; CLU_028880_3_3_11; -.
DR OMA; IGFWGIS; -.
DR PhylomeDB; Q8G845; -.
DR Proteomes; UP000000439; Chromosome.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR001851; ABC_transp_permease.
DR Pfam; PF02653; BPD_transp_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..340
FT /note="Fructose import permease protein FruG"
FT /id="PRO_0000439271"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 340 AA; 35850 MW; A46F22D58F4A82A8 CRC64;
MTTATANKVK APKKGFKLDR QMIPTLAAVV IFILMIIMGQ ALFGTYIRLG FISSLFIDHA
YLIILAVAMT LPILTGGIDL SVGAIVAITA VVGLKLANAG VPAFLVMIIM LLIGAVFGLL
AGTLIEEFNM QPFIATLSTM FLARGLASII STDSLTFPQG NDFSFISNVI KIIDNPKISN
DLSFNVGVII ALVVVVFGYV FLHHTRTGRT IYAIGGSRSS AELMGLPVKR TQYIIYLTSA
TLAALASIVY TANIGSAKNT VGVGWELDAV ASVVIGGTII TGGFGYVLGS VLGSLVRSIL
DPLTSDFGVP AEWTTIVIGL MILVFVVLQR AVMAVGGDKK