ID   DPIA_ECOL6              Reviewed;         226 AA.
AC   P0AEF5; Q54149;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Transcriptional regulatory protein DpiA;
DE   AltName: Full=Destabilizer of plasmid inheritance;
GN   Name=dpiA; Synonyms=citB; OrderedLocusNames=c0711;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Phosphorylated and activated by DpiB. {ECO:0000250}.
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DR   EMBL; AE014075; AAN79184.1; -; Genomic_DNA.
DR   RefSeq; WP_000126500.1; NC_004431.1.
DR   AlphaFoldDB; P0AEF5; -.
DR   SMR; P0AEF5; -.
DR   STRING; 199310.c0711; -.
DR   EnsemblBacteria; AAN79184; AAN79184; c0711.
DR   GeneID; 66671105; -.
DR   KEGG; ecc:c0711; -.
DR   eggNOG; COG4565; Bacteria.
DR   HOGENOM; CLU_000445_39_0_6; -.
DR   OMA; MRHGALQ; -.
DR   BioCyc; ECOL199310:C0711-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Phosphoprotein; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..226
FT                   /note="Transcriptional regulatory protein DpiA"
FT                   /id="PRO_0000081070"
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