ID   FOLT_STRMU              Reviewed;         186 AA.
AC   Q8DV98;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Folate transporter FolT;
DE   AltName: Full=Folate ECF transporter S component FolT;
GN   Name=folT; OrderedLocusNames=SMU_600c;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   FOLATE-BINDING.
RC   STRAIN=ATCC 700610 / UA159;
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; AE014133; AAN58339.1; -; Genomic_DNA.
DR   RefSeq; NP_721033.1; NC_004350.2.
DR   RefSeq; WP_002263248.1; NC_004350.2.
DR   AlphaFoldDB; Q8DV98; -.
DR   SMR; Q8DV98; -.
DR   STRING; 210007.SMU_600c; -.
DR   EnsemblBacteria; AAN58339; AAN58339; SMU_600c.
DR   GeneID; 66817931; -.
DR   KEGG; smu:SMU_600c; -.
DR   PATRIC; fig|210007.7.peg.533; -.
DR   eggNOG; ENOG5033E5K; Bacteria.
DR   HOGENOM; CLU_098232_1_0_9; -.
DR   OMA; ICNIGLN; -.
DR   Proteomes; UP000002512; 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   InterPro; IPR030949; ECF_S_folate_fam.
DR   InterPro; IPR009825; ECF_substrate-spec-like.
DR   Pfam; PF07155; ECF-ribofla_trS; 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..186
FT                   /note="Folate transporter FolT"
FT                   /id="PRO_0000409018"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   186 AA;  21046 MW;  049F372466B024B9 CRC64;
     MNTMFKSPKL SPQRLVTLAM LIALAFAIGK LSIPIIPQQL IISPTFIVNV MIGMIGGPIW
     AFISLAILDI VDNLSSGAGN FIIWWTLLEA VQGLFYGLFF YQKSLSWTNK KDWLHVTIAT
     AIIMLIGSFI FTPLLVQIYY GVPFWAQFAA GRWLKIFEIP IRILVTMAIM PQLQRIPELR
     KLANFK