ID   OMPR_SHIFM              Reviewed;         239 AA.
AC   A0A4P7TS68;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=DNA-binding dual transcriptional regulator OmpR {ECO:0000305};
DE   AltName: Full=Transcriptional regulatory protein OmpR {ECO:0000305};
GN   Name=ompR; ORFNames=EKN05_021990;
OS   Shigella flexneri serotype 5a (strain M90T).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=1086030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M90T / Serotype 5a;
RA   Cervantes-Rivera R., Puhar A.;
RT   "Complete genome sequence and annotation of the laboratory reference strain
RT   Shigella flexneri 5a M90T and genome-wide transcription start site
RT   determination.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M90T / Serotype 5a;
RX   PubMed=2121709; DOI=10.1128/jb.172.11.6274-6281.1990;
RA   Bernardini M.L., Fontaine A., Sansonetti P.J.;
RT   "The two-component regulatory system ompR-envZ controls the virulence of
RT   Shigella flexneri.";
RL   J. Bacteriol. 172:6274-6281(1990).
RN   [3]
RP   FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M90T / Serotype 5a;
RX   PubMed=8359885; DOI=10.1128/iai.61.9.3625-3635.1993;
RA   Bernardini M.L., Sanna M.G., Fontaine A., Sansonetti P.J.;
RT   "OmpC is involved in invasion of epithelial cells by Shigella flexneri.";
RL   Infect. Immun. 61:3625-3635(1993).
CC   -!- FUNCTION: Member of the two-component regulatory system EnvZ/OmpR
CC       involved in regulating expression of the outer membrane porins OmpC and
CC       OmpF as well as other genes. Unlike E.coli, OmpC is expressed at both
CC       low and high osmolarity, while OmpF is expressed at low osmolarity
CC       (PubMed:8359885). This two-component system plays a role in virulence
CC       (PubMed:2121709, PubMed:8359885). Virulence genes of the vir locus are
CC       up-regulated within 30 minutes upon growth in high osmolarity medium
CC       (PubMed:2121709). {ECO:0000269|PubMed:2121709,
CC       ECO:0000269|PubMed:8359885}.
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}.
CC   -!- DISRUPTION PHENOTYPE: A double ompR-envZ deletion invades HeLa cells
CC       less well than the single mutant, has a limited ability to multiply in
CC       host cells and does not cause keratoconjunctivitis in guinea pigs
CC       (PubMed:2121709). A double ompR-envZ deletion has a lowered rate of
CC       infection of HeLa cells. Bacteria are seriously impaired in their
CC       ability to spread between host cells. The double deletion strain
CC       expresses very low amounts of OmpC and no OmpF (PubMed:8359885).
CC       {ECO:0000269|PubMed:2121709, ECO:0000269|PubMed:8359885}.
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DR   EMBL; CP037923; QCC33844.1; -; Genomic_DNA.
DR   RefSeq; WP_001157751.1; NZ_CM001474.1.
DR   AlphaFoldDB; A0A4P7TS68; -.
DR   SMR; A0A4P7TS68; -.
DR   EnsemblBacteria; QCC33844; QCC33844; EKN05_021990.
DR   GeneID; 8912757; -.
DR   Proteomes; UP000296678; 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   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Phosphoprotein; Repressor;
KW   Stress response; Transcription; Transcription regulation;
KW   Two-component regulatory system; Virulence.
FT   CHAIN           1..239
FT                   /note="DNA-binding dual transcriptional regulator OmpR"
FT                   /id="PRO_0000448907"
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