ID   TDCC_YERE8              Reviewed;         442 AA.
AC   A1JIM8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Threonine/serine transporter TdcC {ECO:0000255|HAMAP-Rule:MF_01583};
DE   AltName: Full=H(+)/threonine-serine symporter {ECO:0000255|HAMAP-Rule:MF_01583};
GN   Name=tdcC {ECO:0000255|HAMAP-Rule:MF_01583}; OrderedLocusNames=YE0337;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Involved in the import of threonine and serine into the cell,
CC       with the concomitant import of a proton (symport system).
CC       {ECO:0000255|HAMAP-Rule:MF_01583}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-threonine(in) = H(+)(out) + L-threonine(out);
CC         Xref=Rhea:RHEA:28883, ChEBI:CHEBI:15378, ChEBI:CHEBI:57926;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01583};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28885;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01583};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out);
CC         Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01583};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28889;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01583};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01583}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01583}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       SdaC/TdcC subfamily. {ECO:0000255|HAMAP-Rule:MF_01583}.
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DR   EMBL; AM286415; CAL10467.1; -; Genomic_DNA.
DR   RefSeq; WP_005175589.1; NC_008800.1.
DR   RefSeq; YP_001004715.1; NC_008800.1.
DR   AlphaFoldDB; A1JIM8; -.
DR   SMR; A1JIM8; -.
DR   GeneID; 77329838; -.
DR   KEGG; yen:YE0337; -.
DR   PATRIC; fig|393305.7.peg.432; -.
DR   eggNOG; COG0814; Bacteria.
DR   HOGENOM; CLU_052043_1_1_6; -.
DR   OrthoDB; 1627372at2; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015194; F:L-serine transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015565; F:threonine efflux transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   HAMAP; MF_01583; Thr_Ser_transp_TdcC; 1.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   InterPro; IPR018227; Amino_acid_transport_2.
DR   InterPro; IPR004694; Hydroxy_aa_transpt.
DR   InterPro; IPR023726; Thr/Ser_transpt_TdcC.
DR   NCBIfam; TIGR00814; stp; 1.
DR   PANTHER; PTHR35334; SERINE TRANSPORTER; 1.
DR   PANTHER; PTHR35334:SF1; THREONINE_SERINE TRANSPORTER TDCC; 1.
DR   Pfam; PF01490; Aa_trans; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..442
FT                   /note="Threonine/serine transporter TdcC"
FT                   /id="PRO_0000309176"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
SQ   SEQUENCE   442 AA;  48950 MW;  DFBFC6AF532A7EF1 CRC64;
     MHIDNAITTT IETKTWRKSD TTWTLGLFGT AIGAGVLFFP IRAGFGGLIP ILIMLVLAYP
     IAFLCHRALA RLCLSGSNCS GNITETVEEH FGKTGGVVIT FLYFFAICPL LWIYGVTITN
     TFMTFWENQL QLAPLNRGVV ALALLLLMAV VIYFGKDLMV KVMSFLVFPF IACLVLISLS
     LIPYWNASVI EQVDLSQISL LGHDGILVTV WLGISIMVFS FNFSPIVSSF VVSKREEYEP
     EFGREYTEKK CSQIISRASI LMVAVVMFFA FSCLFTLSPQ NMAEAKAQNI PVLSYLANHF
     SSMAGSRSTF SITLEYAASL IALVAIFKSF FGHYLGTLEG LNGLVIKFGY KGDKTKISSG
     KLNLISMFFI MGSTWLVAYI NPNILDLIEA MGAPIIASLL CLLPMYAIHK LPSLARFRGR
     PENYFVTIVG LLTIFNIVYK LL
//