TDCC_SHIFL
ID TDCC_SHIFL Reviewed; 443 AA.
AC Q83Q28; Q7BZT4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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};
GN OrderedLocusNames=SF3156, S3368;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44627.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18441.1; -; Genomic_DNA.
DR RefSeq; NP_708920.1; NC_004337.2.
DR RefSeq; WP_000107721.1; NZ_WPGW01000077.1.
DR AlphaFoldDB; Q83Q28; -.
DR SMR; Q83Q28; -.
DR STRING; 198214.SF3156; -.
DR EnsemblBacteria; AAN44627; AAN44627; SF3156.
DR EnsemblBacteria; AAP18441; AAP18441; S3368.
DR GeneID; 1027153; -.
DR KEGG; sfl:SF3156; -.
DR KEGG; sfx:S3368; -.
DR PATRIC; fig|198214.7.peg.3746; -.
DR HOGENOM; CLU_052043_1_1_6; -.
DR OMA; SPQNMAE; -.
DR OrthoDB; 369689at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..443
FT /note="Threonine/serine transporter TdcC"
FT /id="PRO_0000309173"
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
