TTDT_ECOUT
ID TTDT_ECOUT Reviewed; 487 AA.
AC Q1R6R8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=L-tartrate/succinate antiporter;
DE AltName: Full=Tartrate carrier;
DE AltName: Full=Tartrate transporter;
GN Name=ttdT; OrderedLocusNames=UTI89_C3499;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- FUNCTION: Catalyzes the uptake of tartrate in exchange for
CC intracellular succinate. Essential for anaerobic L-tartrate
CC fermentation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: Induced by tartrate, via TtdR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC DIT1 subfamily. {ECO:0000305}.
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DR EMBL; CP000243; ABE08946.1; -; Genomic_DNA.
DR RefSeq; WP_000804955.1; NC_007946.1.
DR AlphaFoldDB; Q1R6R8; -.
DR SMR; Q1R6R8; -.
DR EnsemblBacteria; ABE08946; ABE08946; UTI89_C3499.
DR KEGG; eci:UTI89_C3499; -.
DR HOGENOM; CLU_005170_7_0_6; -.
DR OMA; YAWHFFA; -.
DR Proteomes; UP000001952; 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:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR InterPro; IPR030676; CitT-rel.
DR InterPro; IPR001898; SLC13A/DASS.
DR PANTHER; PTHR42826; PTHR42826; 1.
DR Pfam; PF00939; Na_sulph_symp; 1.
DR PIRSF; PIRSF002457; DASS; 1.
DR TIGRFAMs; TIGR00785; dass; 1.
PE 3: Inferred from homology;
KW Antiport; Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..487
FT /note="L-tartrate/succinate antiporter"
FT /id="PRO_0000262714"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 487 AA; 52943 MW; 82CB49D925AEB2FE CRC64;
MKPSTEWWRY LAPLAVIAII ALLPLPAGLE SHTWLYFAVF TGVIVGLILE PVPGAVVAMV
GISIIAILSP WLLFSPEQLA QPGFKFTAKS LSWAVSGFSN SVIWLIFAAF MFGTGYEKTG
LGRRIALILV KKMGHRTLFL GYAVMFSELI LAPVTPSNSA RGAGIIYPII RNLPPLYQSQ
PNDSSSRSIG SYIMWMGIVA DCVTSAIFLT AMAPNLLLIG LMKSASNATL SWGDWFLGML
PLSILLVLLV PWLAYVLYPP ILKSGDQVPR WAETELQAMG PLCSREKRML GLMVGALVLW
IFGGDYIDAA MVGYSVVALM LLLRIICWDD IVSNKAAWNV FFWLASLITL ATGLNNTGFI
SWFGKLLAGS LSGYSPTIVM VALIVVFYLL RYFFASATAY TSALAPMMIA AALAMPEIPL
PVFCLMVGAA IGLGSILTPY ATGPSPIYYG SGYLPTVDYW RLGAIFGLIF LVLLVITGLL
WMPMVLL