TDCC_ECOLI
ID TDCC_ECOLI Reviewed; 443 AA.
AC P0AAD8; P11867; Q2M991;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
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, ECO:0000303|PubMed:3053659};
GN OrderedLocusNames=b3116, JW3087;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2660107; DOI=10.1093/nar/17.10.3994;
RA Schweizer H., Datta P.;
RT "The complete nucleotide sequence of the tdc region of Escherichia coli.";
RL Nucleic Acids Res. 17:3994-3994(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=3053659; DOI=10.1128/jb.170.11.5352-5359.1988;
RA Goss T.J., Schweizer H.P., Datta P.;
RT "Molecular characterization of the tdc operon of Escherichia coli K-12.";
RL J. Bacteriol. 170:5352-5359(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION AS A THREONINE AND SERINE TRANSPORTER, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=2115866; DOI=10.1128/jb.172.8.4288-4294.1990;
RA Sumantran V.N., Schweizer H.P., Datta P.;
RT "A novel membrane-associated threonine permease encoded by the tdcC gene of
RT Escherichia coli.";
RL J. Bacteriol. 172:4288-4294(1990).
RN [6]
RP FUNCTION AS A SERINE TRANSPORTER, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=9498571; DOI=10.1093/oxfordjournals.jbchem.a021887;
RA Ogawa W., Kayahara T., Tsuda M., Mizushima T., Tsuchiya T.;
RT "Isolation and characterization of an Escherichia coli mutant lacking the
RT major serine transporter, and cloning of a serine transporter gene.";
RL J. Biochem. 122:1241-1245(1997).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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, ECO:0000269|PubMed:2115866,
CC ECO:0000269|PubMed:9498571}.
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 ECO:0000269|PubMed:2115866};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28885;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01583,
CC ECO:0000269|PubMed:2115866};
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 ECO:0000269|PubMed:9498571, ECO:0000305|PubMed:2115866};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01583,
CC ECO:0000269|PubMed:9498571, ECO:0000305|PubMed:2115866};
CC -!- ACTIVITY REGULATION: Inhibited by the proton ionophore carbonyl cyanide
CC m-chlorophenylhydrazone (CCCP) (PubMed:2115866, PubMed:9498571).
CC Partially inhibited by the respiratory chain inhibitor KCN
CC (PubMed:2115866). Activity is Na(+) independent (PubMed:2115866,
CC PubMed:9498571). {ECO:0000269|PubMed:2115866,
CC ECO:0000269|PubMed:9498571}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for L-threonine {ECO:0000269|PubMed:2115866};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01583, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:2115866}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01583}.
CC -!- INDUCTION: Induced in amino acid-rich medium under anaerobic
CC conditions. {ECO:0000269|PubMed:2115866}.
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; X14430; CAA32594.1; -; Genomic_DNA.
DR EMBL; M23638; AAA24662.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57920.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76151.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77165.1; -; Genomic_DNA.
DR PIR; A65101; BVECTC.
DR RefSeq; NP_417586.1; NC_000913.3.
DR RefSeq; WP_000107723.1; NZ_LN832404.1.
DR AlphaFoldDB; P0AAD8; -.
DR SMR; P0AAD8; -.
DR BioGRID; 4262418; 8.
DR DIP; DIP-48056N; -.
DR IntAct; P0AAD8; 1.
DR STRING; 511145.b3116; -.
DR TCDB; 2.A.42.2.2; the hydroxy/aromatic amino acid permease (haaap) family.
DR PaxDb; P0AAD8; -.
DR PRIDE; P0AAD8; -.
DR EnsemblBacteria; AAC76151; AAC76151; b3116.
DR EnsemblBacteria; BAE77165; BAE77165; BAE77165.
DR GeneID; 58462233; -.
DR GeneID; 947629; -.
DR KEGG; ecj:JW3087; -.
DR KEGG; eco:b3116; -.
DR PATRIC; fig|1411691.4.peg.3614; -.
DR EchoBASE; EB0984; -.
DR eggNOG; COG0814; Bacteria.
DR HOGENOM; CLU_052043_1_1_6; -.
DR OMA; SPQNMAE; -.
DR PhylomeDB; P0AAD8; -.
DR BioCyc; EcoCyc:TDCC-MON; -.
DR BioCyc; MetaCyc:TDCC-MON; -.
DR PRO; PR:P0AAD8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015195; F:L-threonine transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015565; F:threonine efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IMP:EcoliWiki.
DR GO; GO:0015825; P:L-serine transport; IMP:EcoCyc.
DR GO; GO:0015826; P:threonine transport; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000093812"
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"
FT CONFLICT 70
FT /note="Missing (in Ref. 1; CAA32594 and 2; AAA24662)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..443
FT /note="GLLTILNIVYKLF -> VC (in Ref. 1; CAA32594 and 2;
FT AAA24662)"
FT /evidence="ECO:0000305"
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
