DPIA_ECOLI
ID DPIA_ECOLI Reviewed; 226 AA.
AC P0AEF4; Q54149;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transcriptional regulatory protein DpiA;
DE AltName: Full=Destabilizer of plasmid inheritance;
GN Name=dpiA; Synonyms=citB, criR, mpdA; OrderedLocusNames=b0620, JW0612;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9701802; DOI=10.1046/j.1365-2958.1998.00895.x;
RA Ingmer H., Miller C.A., Cohen S.N.;
RT "Destabilized inheritance of pSC101 and other Escherichia coli plasmids by
RT DpiA, a novel two-component system regulator.";
RL Mol. Microbiol. 29:49-59(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=18997424; DOI=10.1271/bbb.80301;
RA Yamamoto K., Matsumoto F., Oshima T., Fujita N., Ogasawara N., Ishihama A.;
RT "Anaerobic regulation of citrate fermentation by CitAB in Escherichia
RT coli.";
RL Biosci. Biotechnol. Biochem. 72:3011-3014(2008).
RN [7]
RP FUNCTION, PHOSPHORYLATION, AND DNA-BINDING.
RX PubMed=19202292; DOI=10.1271/bbb.80586;
RA Yamamoto K., Matsumoto F., Minagawa S., Oshima T., Fujita N., Ogasawara N.,
RA Ishihama A.;
RT "Characterization of CitA-CitB signal transduction activating genes
RT involved in anaerobic citrate catabolism in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 73:346-350(2009).
CC -!- FUNCTION: Member of the two-component regulatory system DpiA/DpiB,
CC which is essential for expression of citrate-specific fermentation
CC genes and genes involved in plasmid inheritance. Could be involved in
CC response to both the presence of citrate and external redox conditions.
CC Regulates the transcription of citCDEFXGT, dpiAB, mdh and exuT. Binds
CC specifically to the dpiB-citC intergenic region.
CC {ECO:0000269|PubMed:18997424, ECO:0000269|PubMed:19202292}.
CC -!- INTERACTION:
CC P0AEF4; P76079: paaC; NbExp=4; IntAct=EBI-1119284, EBI-1131666;
CC P0AEF4; P39409: yjjW; NbExp=2; IntAct=EBI-1119284, EBI-9132384;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated and activated by DpiB.
CC {ECO:0000269|PubMed:19202292}.
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DR EMBL; U46667; AAC28952.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40820.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73721.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35256.1; -; Genomic_DNA.
DR PIR; B64796; B64796.
DR RefSeq; NP_415153.1; NC_000913.3.
DR RefSeq; WP_000126500.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P0AEF4; -.
DR SMR; P0AEF4; -.
DR BioGRID; 4263364; 6.
DR BioGRID; 851347; 8.
DR DIP; DIP-47831N; -.
DR IntAct; P0AEF4; 15.
DR STRING; 511145.b0620; -.
DR iPTMnet; P0AEF4; -.
DR jPOST; P0AEF4; -.
DR PaxDb; P0AEF4; -.
DR PRIDE; P0AEF4; -.
DR EnsemblBacteria; AAC73721; AAC73721; b0620.
DR EnsemblBacteria; BAA35256; BAA35256; BAA35256.
DR GeneID; 66671105; -.
DR GeneID; 947008; -.
DR KEGG; ecj:JW0612; -.
DR KEGG; eco:b0620; -.
DR PATRIC; fig|511145.12.peg.650; -.
DR EchoBASE; EB3314; -.
DR eggNOG; COG4565; Bacteria.
DR HOGENOM; CLU_000445_39_0_6; -.
DR InParanoid; P0AEF4; -.
DR OMA; MRHGALQ; -.
DR PhylomeDB; P0AEF4; -.
DR BioCyc; EcoCyc:G6346-MON; -.
DR PRO; PR:P0AEF4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR024187; Sig_transdc_resp-reg_cit/mal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR028141; Transcriptional_reg_dom.
DR PANTHER; PTHR45526; PTHR45526; 1.
DR Pfam; PF12431; CitT; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF006171; RR_citrat_malat; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..226
FT /note="Transcriptional regulatory protein DpiA"
FT /id="PRO_0000081068"
FT DOMAIN 6..122
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 180..199
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 226 AA; 25453 MW; 2A47279EED145743 CRC64;
MTAPLTLLIV EDETPLAEMH AEYIRHIPGF SQILLAGNLA QARMMIERFK PGLILLDNYL
PDGRGINLLH ELVQAHYPGD VVFTTAASDM ETVSEAVRCG VFDYLIKPIA YERLGQTLTR
FRQRKHMLES IDSASQKQID EMFNAYARGE PKDELPTGID PLTLNAVRKL FKEPGVQHTA
ETVAQALTIS RTTARRYLEY CASRHLIIAE IVHGKVGRPQ RIYHSG
