ID   FRCC_RHIML              Reviewed;         360 AA.
AC   Q9F9B1;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Fructose import permease protein FrcC {ECO:0000305};
GN   Name=frcC {ECO:0000303|PubMed:11466273};
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=SU47 / Rm5000;
RX   PubMed=11466273; DOI=10.1128/jb.183.16.4709-4717.2001;
RA   Lambert A., Osteras M., Mandon K., Poggi M.C., Le Rudulier D.;
RT   "Fructose uptake in Sinorhizobium meliloti is mediated by a high-affinity
RT   ATP-binding cassette transport system.";
RL   J. Bacteriol. 183:4709-4717(2001).
CC   -!- FUNCTION: Part of the high-affinity ABC transporter complex FrcBCA
CC       involved in fructose uptake. Is also a high-affinity transporter for
CC       ribose and mannose (PubMed:11466273). Responsible for the translocation
CC       of the substrate across the membrane (Probable).
CC       {ECO:0000269|PubMed:11466273, ECO:0000305}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (FrcA),
CC       two transmembrane proteins (FrcC) and a solute-binding protein (FrcB).
CC       {ECO:0000305|PubMed:11466273}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Induced by fructose. {ECO:0000269|PubMed:11466273}.
CC   -!- DISRUPTION PHENOTYPE: Disruption mutant is unable to grow on fructose
CC       as sole carbon source, but can still grow with ribose and mannose as
CC       sole carbon source. {ECO:0000269|PubMed:11466273}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; AF196574; AAG28499.1; -; Genomic_DNA.
DR   RefSeq; WP_003531509.1; NZ_WISY01000026.1.
DR   AlphaFoldDB; Q9F9B1; -.
DR   STRING; 382.DU99_02550; -.
DR   TCDB; 3.A.1.2.7; the atp-binding cassette (abc) superfamily.
DR   GeneID; 61601953; -.
DR   PATRIC; fig|382.52.peg.515; -.
DR   OMA; HTAWGRH; -.
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 inner membrane; Cell membrane; Membrane; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..360
FT                   /note="Fructose import permease protein FrcC"
FT                   /id="PRO_0000439251"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   360 AA;  38176 MW;  00988BDB13486B2E CRC64;
     MGETNTAAQP SQEFEKVLAD SSTDVASFDA HDKTLLQKLQ HFLHSSPAAV PLIVLVLSLI
     AFGVILGGKF FSAFTMTLIL QQVAIVGIVG AAQTLVILTA GIDLSVGAIM VLSSVIMGQF
     TFRYGFPPAL SVICGLGVGA LCGYINGTLV ARMKLPPFIV TLGMWQIVLA SNFLYSANET
     IRAQDISANA SILQFFGQNF RIGNAVFTYG VVVMVLLVCL LWYVLNRTAW GRYVYAVGDD
     PEAAKLAGVN VTRMLISIYT LSGLICALAG WALIGRIGSV SPTAGQFANI ESITAVVIGG
     ISLFGGRGSI MGMLFGALIV GVFSLGLRLM GTDPQWTYLL IGLLIIIAVA IDQWIRKVAA