FRUE_BIFLO
ID FRUE_BIFLO Reviewed; 327 AA.
AC Q8G848;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Fructose import binding protein FruE {ECO:0000305};
DE Flags: Precursor;
GN Name=fruE {ECO:0000303|PubMed:22102285};
GN OrderedLocusNames=BL0033 {ECO:0000312|EMBL:AAN23900.1};
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, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH
RP FRUF AND FRUG, INDUCTION, AND DISRUPTION PHENOTYPE.
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. Binds fructose, ribose and xylose, with fructose as the
CC preferred substrate. {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:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Induced specifically and reversibly by fructose both in a
CC time- and dose-dependent manner. Also induced by ribose or xylose, but
CC not by glucose. {ECO:0000269|PubMed:22102285}.
CC -!- DISRUPTION PHENOTYPE: Mutant is unable to grow on fructose as sole
CC carbon source. {ECO:0000269|PubMed:22102285}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; AE014295; AAN23900.1; -; Genomic_DNA.
DR RefSeq; NP_695264.1; NC_004307.2.
DR RefSeq; WP_007053222.1; NC_004307.2.
DR AlphaFoldDB; Q8G848; -.
DR SMR; Q8G848; -.
DR STRING; 206672.BL0033; -.
DR TCDB; 3.A.1.2.23; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAN23900; AAN23900; BL0033.
DR KEGG; blo:BL0033; -.
DR PATRIC; fig|206672.9.peg.35; -.
DR HOGENOM; CLU_037628_3_2_11; -.
DR OMA; IAVLMYG; -.
DR PhylomeDB; Q8G848; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Sugar transport; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..327
FT /note="Fructose import binding protein FruE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5004307638"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 327 AA; 34690 MW; 9BAD65078CA8A210 CRC64;
MKNWKKAIAL VASAAALVSV AACGSSNAGG SSDSGKKTVG FVAVGPEGGF RTANEKDIQK
AFEDAGFDLT YSPTQNNDQQ KQIQAFNKFV NDEVDAIILS STEDSGWDDS LKKAAEAEIP
VFTVDRNVDV KDAEAKKAIV AHIGPSNVWC GEQAAEFVNK NFPDGANGFI LEGPAGLSVV
KDRGTGWGNK VASNVKVLES QSANWSTDEA KTVTAGLLDK YKSDNPQFIF AQNDEMGLGA
AQAVDAAGLK GKVKIITIDG TKNALQALVD GDLSYVIEYN PIFGKETAQA VKDYLDGKTV
EKDIEIESKT FDAASAKEAL DNNTRAY