TDCC_ECO57
ID TDCC_ECO57 Reviewed; 443 AA.
AC P0AAD9; P11867;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Z4468, ECs3996;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58247.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37419.1; -; Genomic_DNA.
DR PIR; C85973; C85973.
DR PIR; D91128; D91128.
DR RefSeq; NP_312023.1; NC_002695.1.
DR RefSeq; WP_000107723.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AAD9; -.
DR SMR; P0AAD9; -.
DR STRING; 155864.EDL933_4337; -.
DR EnsemblBacteria; AAG58247; AAG58247; Z4468.
DR EnsemblBacteria; BAB37419; BAB37419; ECs_3996.
DR GeneID; 58462233; -.
DR GeneID; 916533; -.
DR KEGG; ece:Z4468; -.
DR KEGG; ecs:ECs_3996; -.
DR PATRIC; fig|386585.9.peg.4170; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_052043_1_1_6; -.
DR OMA; SPQNMAE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000093813"
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; 48879 MW; 761E524AEC4D2656 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 GLNGLVLKFG YKGDKTKVSL
GKLNTISMIF IMGSTWVVAY ANPNILDLIE AMGAPIIASL LCLLPMYAIR KAPSLAKYRG
RLDNVFVTVI GLLTILNIVY KLF
