ID   OMPR_ECOL6              Reviewed;         239 AA.
AC   P0AA17; O31133; P03025; P08981; P41405;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=DNA-binding dual transcriptional regulator OmpR {ECO:0000305};
DE   AltName: Full=Transcriptional regulatory protein OmpR {ECO:0000305};
GN   Name=ompR; OrderedLocusNames=c4181;
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 EnvZ/OmpR
CC       involved in osmoregulation (particularly of genes ompF and ompC) as
CC       well as other genes. Plays a central role in both acid and osmotic
CC       stress responses. Binds to the promoter of both ompC and ompF; at low
CC       osmolarity it activates ompF transcription, while at high osmolarity it
CC       represses ompF and activates ompC transcription.
CC       {ECO:0000250|UniProtKB:P0AA16}.
CC   -!- SUBUNIT: Monomer and multimer. {ECO:0000250|UniProtKB:P0AA16}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AA16}.
CC   -!- PTM: Phosphorylated by EnvZ; this stimulates its DNA-binding ability.
CC       Asp-55 is the primary phosphate acceptor site.
CC       {ECO:0000250|UniProtKB:P0AA16}.
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DR   EMBL; AE014075; AAN82619.1; -; Genomic_DNA.
DR   RefSeq; WP_001157751.1; NC_004431.1.
DR   AlphaFoldDB; P0AA17; -.
DR   SMR; P0AA17; -.
DR   STRING; 199310.c4181; -.
DR   PRIDE; P0AA17; -.
DR   EnsemblBacteria; AAN82619; AAN82619; c4181.
DR   GeneID; 8912757; -.
DR   KEGG; ecc:c4181; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_4_6; -.
DR   OMA; NIHGEGF; -.
DR   BioCyc; ECOL199310:C4181-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:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00383; trans_reg_C; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR039420; WalR-like.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR48111; PTHR48111; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00486; Trans_reg_C; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00862; Trans_reg_C; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS51755; OMPR_PHOB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Phosphoprotein; Repressor;
KW   Stress response; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..239
FT                   /note="DNA-binding dual transcriptional regulator OmpR"
FT                   /id="PRO_0000081177"
FT   DOMAIN          6..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        135..234
FT                   /note="OmpR/PhoB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AA16,
FT                   ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   239 AA;  27354 MW;  823CA7720E9A1D2A CRC64;
     MQENYKILVV DDDMRLRALL ERYLTEQGFQ VRSVANAEQM DRLLTRESFH LMVLDLMLPG
     EDGLSICRRL RSQSNPMPII MVTAKGEEVD RIVGLEIGAD DYIPKPFNPR ELLARIRAVL
     RRQANELPGA PSQEEAVIAF GKFKLNLGTR EMFREDEPMP LTSGEFAVLK ALVSHPREPL
     SRDKLMNLAR GREYSAMERS IDVQISRLRR MVEEDPAHPR YIQTVWGLGY VFVPDGSKA