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TDCC_ECOLC
ID   TDCC_ECOLC              Reviewed;         443 AA.
AC   B1IRJ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=EcolC_0582;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA76258.1; -; Genomic_DNA.
DR   RefSeq; WP_000107721.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IRJ9; -.
DR   SMR; B1IRJ9; -.
DR   KEGG; ecl:EcolC_0582; -.
DR   HOGENOM; CLU_052043_1_1_6; -.
DR   OMA; SPQNMAE; -.
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; IPR018227; Amino_acid_transport_2.
DR   InterPro; IPR004694; Hydroxy_aa_transpt.
DR   InterPro; IPR023726; Thr/Ser_transpt_TdcC.
DR   PANTHER; PTHR35334:SF1; PTHR35334:SF1; 1.
DR   Pfam; PF03222; Trp_Tyr_perm; 1.
DR   TIGRFAMs; TIGR00814; stp; 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_1000087941"
FT   TRANSMEM        22..42
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        97..117
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        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
FT   TRANSMEM        389..409
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;  48893 MW;  B3BDFF795472F0AC CRC64;
     MSTSDSIVSS QTKQSSWRKS DTTWTLGLFG TAIGAGVLFF PIRAGFGGLI PILLMLVLAY
     PIAFYCHRAL ARLCLSGSNP SGNITETVEE HFGKTGGVVI TFLYFFAICP LLWIYGVTIT
     NTFMTFWENQ LGFAPLNRGF VALFLLLLMA FVIWFGKDLM VKVMSYLVWP FIASLVLISL
     SLIPYWNSAV IDQVDLGSLS LTGHDGILIT VWLGISIMVF SFNFSPIVSS FVVSKREEYE
     KDFGRDFTER KCSQIISRAS MLMVAVVMFF AFSCLFTLSP ANMAEAKAQN IPVLSYLANH
     FASMTGTKTT FAITLEYAAS IIALVAIFKS FFGHYLGTLE GLNGLILKFG YKGDKTKVSL
     GKLNTLSMIF IMGSTWVVAY ANPNILDLIE AMGAPIIASL LCLLPMYAIR KAPSLAKYRG
     RLDNVFVTVI GLLTILNIVY KLF
 
 
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