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OMPR_SALTI
ID   OMPR_SALTI              Reviewed;         239 AA.
AC   P0AA20; O31133; P03025; P08981; P41405;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=DNA-binding dual transcriptional regulator OmpR {ECO:0000305};
DE   AltName: Full=Transcriptional regulatory protein OmpR {ECO:0000303|PubMed:8063417};
GN   Name=ompR {ECO:0000303|PubMed:8063417};
GN   Synonyms=ompB {ECO:0000303|PubMed:8063417};
GN   OrderedLocusNames=STY4294, t4004;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN VIRULENCE, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 700931 / Ty2 / CVD908;
RX   PubMed=8063417; DOI=10.1128/iai.62.9.3984-3993.1994;
RA   Pickard D.J., Li J., Roberts M.R., Maskell D., Hone D., Levine M.,
RA   Dougan G., Chatfield S.;
RT   "Characterization of defined ompR mutants of Salmonella typhi: ompR is
RT   involved in the regulation of Vi polysaccharide expression.";
RL   Infect. Immun. 62:3984-3993(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IMSS-1;
RA   Martinez-Flores I., Bustamante V., Puente J.L., Calva E.;
RT   "Cloning and characterization of the Salmonella typhi ompR and envZ
RT   genes.";
RL   Asia Pac. J. Mol. Biol. Biotechnol. 3:135-144(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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 or S.typhimurium both porins
CC       are expressed constitutively. Involved in regulation of the
CC       biosynthesis of Vi polysaccharide, a capsular antigen thought to be
CC       involved in the virulence of S.typhi. Vi antigen is synthesized at low
CC       NaCl concentrations (under 0.4 M) (PubMed:8063417). Binds to the
CC       promoter of both ompC and ompF (By similarity).
CC       {ECO:0000250|UniProtKB:P0AA16, ECO:0000269|PubMed:8063417}.
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: Loss of expression of OmpC and OmpF under low and
CC       high osmolarity. No longer agglutinates with Vi antiserum, agglutinates
CC       with 09 antiserum without boiling, indicating the Vi polysaccharide is
CC       not masking the lipopolysaccharide antigen.
CC       {ECO:0000269|PubMed:8063417}.
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DR   EMBL; X78270; CAA55076.1; -; Genomic_DNA.
DR   EMBL; X77305; CAA54510.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD08112.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71474.1; -; Genomic_DNA.
DR   PIR; S41887; S41887.
DR   RefSeq; NP_458402.1; NC_003198.1.
DR   RefSeq; WP_001157751.1; NZ_WSUR01000001.1.
DR   AlphaFoldDB; P0AA20; -.
DR   SMR; P0AA20; -.
DR   STRING; 220341.16505091; -.
DR   EnsemblBacteria; AAO71474; AAO71474; t4004.
DR   GeneID; 8912757; -.
DR   KEGG; stt:t4004; -.
DR   KEGG; sty:STY4294; -.
DR   PATRIC; fig|220341.7.peg.4388; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_30_4_6; -.
DR   OMA; NIHGEGF; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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.
FT   CHAIN           1..239
FT                   /note="DNA-binding dual transcriptional regulator OmpR"
FT                   /id="PRO_0000081179"
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"
FT   CONFLICT        118
FT                   /note="A -> P (in Ref. 1; CAA55076)"
FT                   /evidence="ECO:0000305"
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
 
 
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