ID   FOLT_CLONN              Reviewed;         172 AA.
AC   A0Q1J7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Folate transporter FolT;
DE   AltName: Full=Folate ECF transporter S component FolT;
GN   Name=folT; OrderedLocusNames=NT01CX_2426;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
RN   [2]
RP   FOLATE-BINDING.
RC   STRAIN=NT;
RX   PubMed=18776013; DOI=10.1128/jb.01070-08;
RA   Eudes A., Erkens G.B., Slotboom D.J., Rodionov D.A., Naponelli V.,
RA   Hanson A.D.;
RT   "Identification of genes encoding the folate- and thiamine-binding membrane
RT   proteins in Firmicutes.";
RL   J. Bacteriol. 190:7591-7594(2008).
CC   -!- FUNCTION: Folate-binding protein that interacts with the energy-
CC       coupling factor (ECF) ABC-transporter complex. Unlike classic ABC
CC       transporters this ECF transporter provides the energy necessary to
CC       transport a number of different substrates. The substrates themselves
CC       are bound by transmembrane, not extracytoplasmic soluble proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter
CC       complex composed of a membrane-embedded substrate-binding protein (S
CC       component), two ATP-binding proteins (A components) and a transmembrane
CC       protein (T component). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; CP000382; ABK62097.1; -; Genomic_DNA.
DR   RefSeq; WP_011722493.1; NC_008593.1.
DR   AlphaFoldDB; A0Q1J7; -.
DR   SMR; A0Q1J7; -.
DR   STRING; 386415.NT01CX_2426; -.
DR   EnsemblBacteria; ABK62097; ABK62097; NT01CX_2426.
DR   KEGG; cno:NT01CX_2426; -.
DR   eggNOG; COG3601; Bacteria.
DR   HOGENOM; CLU_098232_3_0_9; -.
DR   OMA; WLHIMYG; -.
DR   OrthoDB; 1784202at2; -.
DR   Proteomes; UP000008220; 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:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR030949; ECF_S_folate_fam.
DR   InterPro; IPR024529; ECF_trnsprt_substrate-spec.
DR   Pfam; PF12822; ECF_trnsprt; 1.
DR   TIGRFAMs; TIGR04518; ECF_S_folT_fam; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Folate-binding; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..172
FT                   /note="Folate transporter FolT"
FT                   /id="PRO_0000409015"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   172 AA;  19156 MW;  D2CE34938FB2CD70 CRC64;
     MKKVNVMIYM AFMITLEIVF TRFLSIQTPI IRIGFGFIPV AMSGMMFGPL LAGIVGATSD
     VLGMMIFPKG AYFPGFTLSA FVGAVIYGVF FYNKKVSVKR VLLAVGIITV LVNLTMNTIW
     LQILTGKAVK VLFVTRLVKE AIMFPIHAIV IYGAWKMVDR LEIMNKVAKF NK