DCTA_ECOLI
ID DCTA_ECOLI Reviewed; 428 AA.
AC P0A830; P37312; Q2M7J0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Aerobic C4-dicarboxylate transport protein;
GN Name=dctA; OrderedLocusNames=b3528, JW3496;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
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 [3]
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 [4]
RP CHARACTERIZATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10482502; DOI=10.1128/jb.181.18.5624-5635.1999;
RA Davies S.J., Golby P., Omrani D., Broad S.A., Harrington V.L., Guest J.R.,
RA Kelly D.J., Andrews S.C.;
RT "Inactivation and regulation of the aerobic C(4)-dicarboxylate transport
RT (dctA) gene of Escherichia coli.";
RL J. Bacteriol. 181:5624-5635(1999).
RN [5]
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).
RN [6]
RP FUNCTION AS A D-MALATE TRANSPORTER, ROLE IN D-MALATE UTILIZATION,
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=17088549; DOI=10.1073/pnas.0603364103;
RA Reed J.L., Patel T.R., Chen K.H., Joyce A.R., Applebee M.K., Herring C.D.,
RA Bui O.T., Knight E.M., Fong S.S., Palsson B.O.;
RT "Systems approach to refining genome annotation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17480-17484(2006).
CC -!- FUNCTION: Responsible for the aerobic transport of the dicarboxylates
CC fumarate, L- and D-malate and to a lesser extent succinate, from the
CC periplasm across the inner membrane. {ECO:0000269|PubMed:17088549}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Subject to CRP-mediated catabolite repression. Repressed in
CC the absence of oxygen, induced in the stationary phase and
CC approximately 2-fold by citrate and C4-dicarboxylates.
CC {ECO:0000269|PubMed:17088549}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are only able to grow
CC after a 2-day lag period on D-malate as sole carbon source.
CC {ECO:0000269|PubMed:17088549}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000305}.
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DR EMBL; U00039; AAB18505.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76553.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77766.1; -; Genomic_DNA.
DR PIR; S47749; S47749.
DR RefSeq; NP_417985.1; NC_000913.3.
DR RefSeq; WP_000858214.1; NZ_STEB01000018.1.
DR AlphaFoldDB; P0A830; -.
DR SMR; P0A830; -.
DR BioGRID; 4262159; 13.
DR DIP; DIP-47958N; -.
DR IntAct; P0A830; 1.
DR STRING; 511145.b3528; -.
DR TCDB; 2.A.23.1.7; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR jPOST; P0A830; -.
DR PaxDb; P0A830; -.
DR PRIDE; P0A830; -.
DR EnsemblBacteria; AAC76553; AAC76553; b3528.
DR EnsemblBacteria; BAE77766; BAE77766; BAE77766.
DR GeneID; 66672587; -.
DR GeneID; 948039; -.
DR KEGG; ecj:JW3496; -.
DR KEGG; eco:b3528; -.
DR PATRIC; fig|1411691.4.peg.3189; -.
DR EchoBASE; EB4140; -.
DR eggNOG; COG1301; Bacteria.
DR HOGENOM; CLU_019375_7_0_6; -.
DR InParanoid; P0A830; -.
DR OMA; YLYIAVI; -.
DR PhylomeDB; P0A830; -.
DR BioCyc; EcoCyc:DCTA-MON; -.
DR BioCyc; MetaCyc:DCTA-MON; -.
DR PRO; PR:P0A830; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015138; F:fumarate transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015366; F:malate:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0015741; P:fumarate transport; IDA:EcoliWiki.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IDA:EcoCyc.
DR Gene3D; 1.10.3860.10; -; 1.
DR HAMAP; MF_01300; C4_dicarb_transport; 1.
DR InterPro; IPR023954; C4_dicarb_transport.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR42865; PTHR42865; 1.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..428
FT /note="Aerobic C4-dicarboxylate transport protein"
FT /id="PRO_0000202094"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 428 AA; 45436 MW; D9B32F987B62D234 CRC64;
MKTSLFKSLY FQVLTAIAIG ILLGHFYPEI GEQMKPLGDG FVKLIKMIIA PVIFCTVVTG
IAGMESMKAV GRTGAVALLY FEIVSTIALI IGLIIVNVVQ PGAGMNVDPA TLDAKAVAVY
ADQAKDQGIV AFIMDVIPAS VIGAFASGNI LQVLLFAVLF GFALHRLGSK GQLIFNVIES
FSQVIFGIIN MIMRLAPIGA FGAMAFTIGK YGVGTLVQLG QLIICFYITC ILFVVLVLGS
IAKATGFSIF KFIRYIREEL LIVLGTSSSE SALPRMLDKM EKLGCRKSVV GLVIPTGYSF
NLDGTSIYLT MAAVFIAQAT NSQMDIVHQI TLLIVLLLSS KGAAGVTGSG FIVLAATLSA
VGHLPVAGLA LILGIDRFMS EARALTNLVG NGVATIVVAK WVKELDHKKL DDVLNNRAPD
GKTHELSS
