DAUA_ECOLI
ID DAUA_ECOLI Reviewed; 559 AA.
AC P0AFR2; P40877; P76019;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=C4-dicarboxylic acid transporter DauA {ECO:0000305};
DE AltName: Full=Dicarboxylic acid uptake system A {ECO:0000303|PubMed:23278959};
GN Name=dauA {ECO:0000303|PubMed:23278959}; Synonyms=ychM;
GN OrderedLocusNames=b1206, JW5189;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-114.
RC STRAIN=K12;
RA Lloyd R.G.;
RL Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-66.
RX PubMed=3009477; DOI=10.1016/s0021-9258(19)62682-7;
RA Hove-Jensen B., Harlow K.W., King C.J., Switzer R.L.;
RT "Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of
RT the purified enzyme and primary structure of the prs gene.";
RL J. Biol. Chem. 261:6765-6771(1986).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP IDENTIFICATION, AND SIMILARITY TO SULFATE PERMEASES.
RX PubMed=8140616; DOI=10.1016/0968-0004(94)90168-6;
RA Sandal N.N., Marcker K.A.;
RT "Similarities between a soybean nodulin, Neurospora crassa sulphate
RT permease II and a putative human tumour suppressor.";
RL Trends Biochem. Sci. 19:19-19(1994).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=K12 / BW25113;
RX PubMed=23278959; DOI=10.1111/mmi.12120;
RA Karinou E., Compton E.L., Morel M., Javelle A.;
RT "The Escherichia coli SLC26 homologue YchM (DauA) is a C(4)-dicarboxylic
RT acid transporter.";
RL Mol. Microbiol. 87:623-640(2013).
RN [10] {ECO:0007744|PDB:3NY7}
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 445-559 IN COMPLEX WITH
RP ACYL-CARRIER PROTEIN, INTERACTION WITH ACP, AND DISRUPTION PHENOTYPE.
RX PubMed=21070944; DOI=10.1016/j.str.2010.08.015;
RA Babu M., Greenblatt J.F., Emili A., Strynadka N.C., Reithmeier R.A.,
RA Moraes T.F.;
RT "Structure of a SLC26 anion transporter STAS domain in complex with acyl
RT carrier protein: implications for E. coli YchM in fatty acid metabolism.";
RL Structure 18:1450-1462(2010).
CC -!- FUNCTION: Responsible for the aerobic transport of succinate from the
CC periplasm to the cytoplasm at acidic pH (PubMed:23278959). Can
CC transport other C4-dicarboxylic acids such as aspartate and fumarate
CC (PubMed:23278959). May also play a role in the regulation of C4-
CC dicarboxylic acid metabolism at pH 7, via regulation of expression
CC and/or activity of DctA. May act as a co-sensor of DcuS
CC (PubMed:23278959). {ECO:0000269|PubMed:23278959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+)(in) + succinate(in) = 2 H(+)(out) + succinate(out);
CC Xref=Rhea:RHEA:29303, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031;
CC Evidence={ECO:0000305|PubMed:23278959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+)(in) + L-aspartate(in) = 2 H(+)(out) + L-aspartate(out);
CC Xref=Rhea:RHEA:29287, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000305|PubMed:23278959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fumarate(in) + 2 H(+)(in) = fumarate(out) + 2 H(+)(out);
CC Xref=Rhea:RHEA:29331, ChEBI:CHEBI:15378, ChEBI:CHEBI:29806;
CC Evidence={ECO:0000305|PubMed:23278959};
CC -!- SUBUNIT: Interacts via the C-terminal cytoplasmic STAS domain with
CC acyl-carrier protein (ACP), an essential component of the fatty acid
CC biosynthesis (FAB) pathway. It also copurifies with proteins involved
CC in fatty acid metabolism. {ECO:0000269|PubMed:21070944}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:23278959}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant is metabolically inactive when succinate
CC is used as sole carbon source. Does not affect growth on glucose,
CC fructose, maltose and glycerol (PubMed:23278959). Deletion mutant shows
CC altered cellular bicarbonate incorporation in the presence of NaCl and
CC impaired growth at alkaline pH (PubMed:21070944).
CC {ECO:0000269|PubMed:21070944, ECO:0000269|PubMed:23278959}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74290.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA36064.2; -; Genomic_DNA.
DR EMBL; X53983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M13174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64867; C64867.
DR RefSeq; NP_415724.2; NC_000913.3.
DR RefSeq; WP_001033352.1; NZ_STEB01000023.1.
DR PDB; 3NY7; X-ray; 1.92 A; A=445-559.
DR PDBsum; 3NY7; -.
DR AlphaFoldDB; P0AFR2; -.
DR SMR; P0AFR2; -.
DR BioGRID; 4259558; 713.
DR DIP; DIP-48160N; -.
DR STRING; 511145.b1206; -.
DR TCDB; 2.A.53.3.11; the sulfate permease (sulp) family.
DR jPOST; P0AFR2; -.
DR PaxDb; P0AFR2; -.
DR PRIDE; P0AFR2; -.
DR EnsemblBacteria; AAC74290; AAC74290; b1206.
DR EnsemblBacteria; BAA36064; BAA36064; BAA36064.
DR GeneID; 66674974; -.
DR GeneID; 945770; -.
DR KEGG; ecj:JW5189; -.
DR KEGG; eco:b1206; -.
DR PATRIC; fig|511145.12.peg.1254; -.
DR EchoBASE; EB2293; -.
DR eggNOG; COG0659; Bacteria.
DR HOGENOM; CLU_003182_13_1_6; -.
DR InParanoid; P0AFR2; -.
DR OMA; VTNKFPI; -.
DR PhylomeDB; P0AFR2; -.
DR BioCyc; EcoCyc:YCHM-MON; -.
DR BioCyc; MetaCyc:YCHM-MON; -.
DR PRO; PR:P0AFR2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015138; F:fumarate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015810; P:aspartate transmembrane transport; IDA:EcoCyc.
DR GO; GO:0015741; P:fumarate transport; IDA:EcoCyc.
DR GO; GO:0071422; P:succinate transmembrane transport; IDA:EcoCyc.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..559
FT /note="C4-dicarboxylic acid transporter DauA"
FT /id="PRO_0000080195"
FT TOPO_DOM 1..32
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..101
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..177
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..278
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..350
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..418
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 449..559
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT CONFLICT 111..114
FT /note="LSGI -> AVGD (in Ref. 4; X53983)"
FT /evidence="ECO:0000305"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:3NY7"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:3NY7"
FT HELIX 470..481
FT /evidence="ECO:0007829|PDB:3NY7"
FT STRAND 488..496
FT /evidence="ECO:0007829|PDB:3NY7"
FT HELIX 502..514
FT /evidence="ECO:0007829|PDB:3NY7"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:3NY7"
FT HELIX 528..536
FT /evidence="ECO:0007829|PDB:3NY7"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:3NY7"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:3NY7"
FT HELIX 552..555
FT /evidence="ECO:0007829|PDB:3NY7"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:3NY7"
SQ SEQUENCE 559 AA; 59429 MW; 14EC83860002F23C CRC64;
MNKIFSSHVM PFRALIDACW KEKYTAARFT RDLIAGITVG IIAIPLAMAL AIGSGVAPQY
GLYTAAVAGI VIALTGGSRF SVSGPTAAFV VILYPVSQQF GLAGLLVATL LSGIFLILMG
LARFGRLIEY IPVSVTLGFT SGIGITIGTM QIKDFLGLQM AHVPEHYLQK VGALFMALPT
INVGDAAIGI VTLGILVFWP RLGIRLPGHL PALLAGCAVM GIVNLLGGHV ATIGSQFHYV
LADGSQGNGI PQLLPQLVLP WDLPNSEFTL TWDSIRTLLP AAFSMAMLGA IESLLCAVVL
DGMTGTKHKA NSELVGQGLG NIIAPFFGGI TATAAIARSA ANVRAGATSP ISAVIHSILV
ILALLVLAPL LSWLPLSAMA ALLLMVAWNM SEAHKVVDLL RHAPKDDIIV MLLCMSLTVL
FDMVIAISVG IVLASLLFMR RIARMTRLAP VVVDVPDDVL VLRVIGPLFF AAAEGLFTDL
ESRLEGKRIV ILKWDAVPVL DAGGLDAFQR FVKRLPEGCE LRVCNVEFQP LRTMARAGIQ
PIPGRLAFFP NRRAAMADL
