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TDCC_EDWTE
ID   TDCC_EDWTE              Reviewed;         443 AA.
AC   D0ZE09;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 54.
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=ETAE_0895;
OS   Edwardsiella tarda (strain EIB202).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=498217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EIB202;
RX   PubMed=19865481; DOI=10.1371/journal.pone.0007646;
RA   Wang Q., Yang M., Xiao J., Wu H., Wang X., Lv Y., Xu L., Zheng H., Wang S.,
RA   Zhao G., Liu Q., Zhang Y.;
RT   "Genome sequence of the versatile fish pathogen Edwardsiella tarda provides
RT   insights into its adaptation to broad host ranges and intracellular
RT   niches.";
RL   PLoS ONE 4:E7646-E7646(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACY83740.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001135; ACY83740.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041692492.1; NC_013508.1.
DR   AlphaFoldDB; D0ZE09; -.
DR   SMR; D0ZE09; -.
DR   EnsemblBacteria; ACY83740; ACY83740; ETAE_0895.
DR   KEGG; etr:ETAE_0895; -.
DR   HOGENOM; CLU_052043_1_1_6; -.
DR   OMA; SPQNMAE; -.
DR   OrthoDB; 369689at2; -.
DR   Proteomes; UP000002634; 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:0022889; F: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   HAMAP; MF_01583; Thr_Ser_transp_TdcC; 1.
DR   InterPro; IPR023726; Thr/Ser_transpt_TdcC.
DR   PANTHER; PTHR35334:SF1; PTHR35334:SF1; 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..443
FT                   /note="Threonine/serine transporter TdcC"
FT                   /id="PRO_0000401181"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
SQ   SEQUENCE   443 AA;  48853 MW;  A637B8C1D1B402F4 CRC64;
     MSSTDSVVAG QAKVTTWRKT DTRWVLGLFG TAIGAGVLFF PISAGIGGLL PIIFMLILAF
     PIAFFCHRAL ARLCLSGRSI SDNITDTVDQ HFGHVGGVVI TFLYFFAICP LLWIYGVTIT
     NTFIAFWQHQ LLLPAINRGV VALAILLVMA FFIYFGKDLM VKVMGYLVFP FITCLVLISL
     SLIPYWTGDI FTSFDMHSLS LFGSHGILVT VWLGIAIMVF SFNFSPIVSS FVVSKREEYE
     ADFGREYTEQ KCAKIISRAS VLMVVVVMFF AFSCLFTLSP QDMAQAKQQN IPILSYLANH
     FSSLGSGKST YATVLEYGAS IIALVAIFKS FFGHYLGTLE GLNGLIIKFG YHGEKSQAPM
     KKLNMISMVI IMGSTWVIAY INPNILDLIG AMGAPIIAAL LCLLPMYAVW RVPALAKYKG
     KASNYFVTII GLLTILNIVY QLM
 
 
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