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TDCC_SALPB
ID   TDCC_SALPB              Reviewed;         443 AA.
AC   A9N628;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-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=SPAB_04046;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000886; ABX69374.1; -; Genomic_DNA.
DR   RefSeq; WP_000108130.1; NC_010102.1.
DR   AlphaFoldDB; A9N628; -.
DR   KEGG; spq:SPAB_04046; -.
DR   PATRIC; fig|1016998.12.peg.3813; -.
DR   HOGENOM; CLU_052043_1_1_6; -.
DR   OMA; SPQNMAE; -.
DR   BioCyc; SENT1016998:SPAB_RS16435-MON; -.
DR   Proteomes; UP000008556; 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; 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_1000087943"
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        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        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;  48992 MW;  35F1B90EFBBB4744 CRC64;
     MSTTDSIVSS QAKQSSWRKS DTTWTLGLFG TAIGAGVLFF PIRAGFGGLI PILLMLVLAY
     PIAFYCHRAL ARLCLSGSNP SGNITETVEE HFGKTGGVVI TFLYFFAICP LLWIYGVTIT
     NTFMTFWENQ LQMPALNRGF VALFLLLLMA FVIWFGKDLM VKVMSYLVWP FIASLVLISL
     SLIPYWNSAV IDQVDLSNIA LTGHDGILVT VWLGISIMVF SFNFSPIVSS FVVSKREEYE
     KEFGREFTER KCSQIISRAS MLMVAVVMFF AFSCLFTLSP QNMADAKAQN IPVLSYLANH
     FASLSGTKST FATVLEYGAS IIALVAIFKS FFGHYLGTLE GLNGLVMKFG YKGDKTKVSM
     GKLNTISMIF IMGSTWVVAY ANPNILDLIE AMGAPIIASL LCLLPMYAIR KAPSLAKYRG
     RLDNVFVTLI GLLTILNIVY KLF
 
 
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