TDCC_ESCF3
ID TDCC_ESCF3 Reviewed; 443 AA.
AC B7LQI2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=EFER_3049;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ90542.1; -; Genomic_DNA.
DR RefSeq; WP_000099375.1; NC_011740.1.
DR AlphaFoldDB; B7LQI2; -.
DR EnsemblBacteria; CAQ90542; CAQ90542; EFER_3049.
DR KEGG; efe:EFER_3049; -.
DR HOGENOM; CLU_052043_1_1_6; -.
DR OMA; SPQNMAE; -.
DR OrthoDB; 369689at2; -.
DR BioCyc; EFER585054:EFER_RS15370-MON; -.
DR Proteomes; UP000000745; 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_1000147633"
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 135..155
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 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01583"
SQ SEQUENCE 443 AA; 49111 MW; DDCADFA65348A03B CRC64;
MSSTDNIVSG KAQHSYWRKS DTTWTLGLFG TAIGAGVLFF PIRAGFGGLI PILVMLVLAY
PIAFYCHRAL ARLCLSGANP SGNITETVEE HFGKTGGVVI TFLYFFAICP LLWIYGVTIT
NTFMTFWENQ LHLPALNRGF VALFLLLLMA VIIWFGRDLM VKVMSFLVWP FIASLVLISL
SLIPYWNSAV IDQVDLSALS LTGHDGILVT VWLGISIMVF SFNFSPIVSS FVVFKREEYE
KKFGRDFTER KCSKIISRAS ILMVAVVMFF AFSCLFALSP QNMAEAKAQN IPVLSYLANH
FSSMSGSQSS FALTLEYAAS IIALVAIFKS FFGHYLGTLE GLNRLIIKFA YKGDKSKISM
SKLNTLSMVF IMGSTWLVAY VNPNILDLIE AMGAPIIASL LCLLPMYAIH KVPSLAKYRG
RIDNVFVTAI GLLTISNIVY KVF
