OMPR_ECOLI
ID OMPR_ECOLI Reviewed; 239 AA.
AC P0AA16; O31133; P03025; P08981; P41405; Q2M770;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA-binding dual transcriptional regulator OmpR {ECO:0000305};
DE AltName: Full=Transcriptional regulatory protein OmpR {ECO:0000305};
GN Name=ompR; Synonyms=kmt, ompB; OrderedLocusNames=b3405, JW3368;
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 OPERON STRUCTURE.
RX PubMed=6292199; DOI=10.1016/s0021-9258(18)33501-4;
RA Wurtzel E.T., Chou M.-Y., Inouye M.;
RT "Osmoregulation of gene expression. I. DNA sequence of the ompR gene of the
RT ompB operon of Escherichia coli and characterization of its gene product.";
RL J. Biol. Chem. 257:13685-13691(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO 7 AND C-TERMINUS,
RP AND MUTAGENESIS OF ARG-15; ARG-71; ARG-150; 164-GLY--ARG-182 AND VAL-203.
RC STRAIN=K12;
RX PubMed=3010044; DOI=10.1007/bf00331636;
RA Nara F., Matsuyama S., Mizuno T., Mizushima S.;
RT "Molecular analysis of mutant ompR genes exhibiting different phenotypes as
RT to osmoregulation of the ompF and ompC genes of Escherichia coli.";
RL Mol. Gen. Genet. 202:194-199(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 7 AND
RP C-TERMINUS.
RC STRAIN=K12;
RX PubMed=2997120; DOI=10.1128/jb.164.2.578-584.1985;
RA Comeau D.E., Ikenaka K., Tsung K., Inouye M.;
RT "Primary characterization of the protein products of the Escherichia coli
RT ompB locus: structure and regulation of synthesis of the OmpR and EnvZ
RT proteins.";
RL J. Bacteriol. 164:578-584(1985).
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 PROTEIN SEQUENCE OF 1-5, FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=3533941; DOI=10.1016/s0021-9258(18)66860-7;
RA Jo Y.L., Nara F., Ichihara S., Mizuno T., Mizushima S.;
RT "Purification and characterization of the OmpR protein, a positive
RT regulator involved in osmoregulatory expression of the ompF and ompC genes
RT in Escherichia coli.";
RL J. Biol. Chem. 261:15252-15256(1986).
RN [7]
RP PROTEIN SEQUENCE OF 1-5; 193-197 AND 200-204, DOMAIN, PHOSPHORYLATION, AND
RP MASS SPECTROMETRY.
RX PubMed=7568033; DOI=10.1073/pnas.92.19.8866;
RA Kenney L.J., Bauer M.D., Silhavy T.J.;
RT "Phosphorylation-dependent conformational changes in OmpR, an
RT osmoregulatory DNA-binding protein of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8866-8870(1995).
RN [8]
RP PROTEIN SEQUENCE OF 47-58, PHOSPHORYLATION AND DEPHOSPHORYLATION BY ENVZ,
RP PHOSPHORYLATION AT ASP-55, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 11-ASP-ASP-12; ASP-11; ASP-12 AND ASP-55.
RX PubMed=7934854; DOI=10.1111/j.1365-2958.1993.tb00974.x;
RA Delgado J., Forst S., Harlocker S., Inouye M.;
RT "Identification of a phosphorylation site and functional analysis of
RT conserved aspartic acid residues of OmpR, a transcriptional activator for
RT ompF and ompC in Escherichia coli.";
RL Mol. Microbiol. 10:1037-1047(1993).
RN [9]
RP FUNCTION AS A TRANSCRIPTIONAL REGULATOR, AND DNA-BINDING.
RX PubMed=3023382; DOI=10.1016/s0021-9258(19)76006-2;
RA Norioka S., Ramakrishnan G., Ikenaka K., Inouye M.;
RT "Interaction of a transcriptional activator, OmpR, with reciprocally
RT osmoregulated genes, ompF and ompC, of Escherichia coli.";
RL J. Biol. Chem. 261:17113-17119(1986).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF LEU-16.
RX PubMed=3536870; DOI=10.1128/jb.168.3.1309-1314.1986;
RA Matsuyama S., Mizuno T., Mizushima S.;
RT "Interaction between two regulatory proteins in osmoregulatory expression
RT of ompF and ompC genes in Escherichia coli: a novel ompR mutation
RT suppresses pleiotropic defects caused by an envZ mutation.";
RL J. Bacteriol. 168:1309-1314(1986).
RN [11]
RP PHOSPHORYLATION AND DEPHOSPHORYLATION BY ENVZ, AND CROSSTALK BETWEEN
RP TWO-COMPONENT SYSTEMS.
RX PubMed=2558046; DOI=10.1101/gad.3.11.1725;
RA Igo M.M., Ninfa A.J., Stock J.B., Silhavy T.J.;
RT "Phosphorylation and dephosphorylation of a bacterial transcriptional
RT activator by a transmembrane receptor.";
RL Genes Dev. 3:1725-1734(1989).
RN [12]
RP FUNCTION, PHOSPHORYLATION, AND DNA-BINDING.
RX PubMed=2674113; DOI=10.1093/oxfordjournals.jbchem.a122817;
RA Aiba H., Nakasai F., Mizushima S., Mizuno T.;
RT "Phosphorylation of a bacterial activator protein, OmpR, by a protein
RT kinase, EnvZ, results in stimulation of its DNA-binding ability.";
RL J. Biochem. 106:5-7(1989).
RN [13]
RP PHOSPHORYLATION BY ENVZ.
RX PubMed=2656684; DOI=10.1016/s0021-9258(18)81828-2;
RA Aiba H., Mizuno T., Mizushima S.;
RT "Transfer of phosphoryl group between two regulatory proteins involved in
RT osmoregulatory expression of the ompF and ompC genes in Escherichia coli.";
RL J. Biol. Chem. 264:8563-8567(1989).
RN [14]
RP PHOSPHORYLATION AND DEPHOSPHORYLATION BY ENVZ, AND MUTAGENESIS OF ARG-15
RP AND LEU-16.
RX PubMed=2668281; DOI=10.1016/s0021-9258(18)71647-5;
RA Aiba H., Nakasai F., Mizushima S., Mizuno T.;
RT "Evidence for the physiological importance of the phosphotransfer between
RT the two regulatory components, EnvZ and OmpR, in osmoregulation in
RT Escherichia coli.";
RL J. Biol. Chem. 264:14090-14094(1989).
RN [15]
RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR AND REPRESSOR FOR OMPF.
RX PubMed=2557454; DOI=10.1016/0022-2836(89)90330-6;
RA Slauch J.M., Silhavy T.J.;
RT "Genetic analysis of the switch that controls porin gene expression in
RT Escherichia coli K-12.";
RL J. Mol. Biol. 210:281-292(1989).
RN [16]
RP FUNCTION, AND PHOSPHORYLATION BY ENVZ.
RX PubMed=2668953; DOI=10.1073/pnas.86.16.6052;
RA Forst S., Delgado J., Inouye M.;
RT "Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the
RT ompF and ompC genes in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6052-6056(1989).
RN [17]
RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR FOR OMPC, AND DNA-BINDING.
RX PubMed=2403550; DOI=10.1128/jb.172.1.501-503.1990;
RA Maeda S., Mizuno T.;
RT "Evidence for multiple OmpR-binding sites in the upstream activation
RT sequence of the ompC promoter in Escherichia coli: a single OmpR-binding
RT site is capable of activating the promoter.";
RL J. Bacteriol. 172:501-503(1990).
RN [18]
RP PHOSPHORYLATION AND DEPHOSPHORYLATION BY ENVZ, PROBABLE PHOSPHORYLATION AT
RP ASP-55, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-12 AND ASP-55.
RX PubMed=2277041; DOI=10.1093/oxfordjournals.jbchem.a123225;
RA Kanamaru K., Aiba H., Mizuno T.;
RT "Transmembrane signal transduction and osmoregulation in Escherichia coli:
RT I. Analysis by site-directed mutagenesis of the amino acid residues
RT involved in phosphotransfer between the two regulatory components, EnvZ and
RT OmpR.";
RL J. Biochem. 108:483-487(1990).
RN [19]
RP SUBUNIT, AND DNA-BINDING.
RX PubMed=7592927; DOI=10.1074/jbc.270.45.26849;
RA Harlocker S.L., Bergstrom L., Inouye M.;
RT "Tandem binding of six OmpR proteins to the ompF upstream regulatory
RT sequence of Escherichia coli.";
RL J. Biol. Chem. 270:26849-26856(1995).
RN [20]
RP REGULON.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28526842; DOI=10.1038/s41598-017-02110-7;
RA Seo S.W., Gao Y., Kim D., Szubin R., Yang J., Cho B.K., Palsson B.O.;
RT "Revealing genome-scale transcriptional regulatory landscape of OmpR
RT highlights its expanded regulatory roles under osmotic stress in
RT Escherichia coli K-12 MG1655.";
RL Sci. Rep. 7:2181-2181(2017).
RN [21]
RP FUNCTION IN ACID STRESS, SUBUNIT, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=29138484; DOI=10.1038/s41467-017-02030-0;
RA Chakraborty S., Winardhi R.S., Morgan L.K., Yan J., Kenney L.J.;
RT "Non-canonical activation of OmpR drives acid and osmotic stress responses
RT in single bacterial cells.";
RL Nat. Commun. 8:1587-1587(2017).
RN [22]
RP REGULON, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30524381; DOI=10.3389/fmicb.2018.02656;
RA Chakraborty S., Kenney L.J.;
RT "A new role of OmpR in acid and osmotic stress in Salmonella and E. coli.";
RL Front. Microbiol. 9:2656-2656(2018).
RN [23]
RP ACTIVITY REGULATION.
RC STRAIN=K12 / MC4100;
RX PubMed=28423182; DOI=10.1002/1873-3468.12658;
RA Hwang E., Cheong H.K., Kim S.Y., Kwon O., Blain K.Y., Choe S., Yeo K.J.,
RA Jung Y.W., Jeon Y.H., Cheong C.;
RT "Crystal structure of the EnvZ periplasmic domain with CHAPS.";
RL FEBS Lett. 591:1419-1428(2017).
RN [24] {ECO:0007744|PDB:1ODD}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 122-239.
RX PubMed=8989318; DOI=10.1038/nsb0197-28;
RA Kondo H., Nakagawa A., Nishihira J., Nishimura Y., Mizuno T., Tanaka I.;
RT "Escherichia coli positive regulator OmpR has a large loop structure at the
RT putative RNA polymerase interaction site.";
RL Nat. Struct. Biol. 4:28-31(1997).
RN [25] {ECO:0007744|PDB:1OPC}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 130-239.
RX PubMed=9016718; DOI=10.1016/s0969-2126(97)00170-6;
RA Martinez-Hackert E., Stock A.M.;
RT "The DNA-binding domain of OmpR: crystal structures of a winged helix
RT transcription factor.";
RL Structure 5:109-124(1997).
RN [26] {ECO:0007744|PDB:2JPB}
RP STRUCTURE BY NMR OF 136-239, SUBUNIT, MUTAGENESIS OF ARG-207; ARG-209;
RP THR-224; VAL-225 AND TRP-226, AND DNA-BINDING.
RX PubMed=18195018; DOI=10.1074/jbc.m705550200;
RA Rhee J.E., Sheng W., Morgan L.K., Nolet R., Liao X., Kenney L.J.;
RT "Amino acids important for DNA recognition by the response regulator
RT OmpR.";
RL J. Biol. Chem. 283:8664-8677(2008).
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 (PubMed:3010044, PubMed:3536870). Plays a central
CC role in both acid and osmotic stress responses (PubMed:28526842,
CC PubMed:30524381). 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 (PubMed:3533941,
CC PubMed:3023382, PubMed:2557454, PubMed:2403550, PubMed:7592927).
CC Involved in acid stress response; this requires EnvZ but not OmpR
CC phosphorylation (PubMed:29138484). Phosphorylated by EnvZ; this
CC stimulates OmpR's DNA-binding ability (PubMed:2656684, PubMed:2668281,
CC PubMed:2668953, PubMed:2674113, PubMed:2558046, PubMed:7934854). Is
CC also dephosphorylated by EnvZ (PubMed:2668281, PubMed:2558046,
CC PubMed:7934854). A single OmpR protein can bind to DNA; OmpR dimers can
CC form on the DNA in either direction, suggesting that interactions
CC between the 2 DNA-binding domains are weak or absent (PubMed:18195018).
CC {ECO:0000269|PubMed:18195018, ECO:0000269|PubMed:2403550,
CC ECO:0000269|PubMed:2557454, ECO:0000269|PubMed:2558046,
CC ECO:0000269|PubMed:2656684, ECO:0000269|PubMed:2668281,
CC ECO:0000269|PubMed:2668953, ECO:0000269|PubMed:2674113,
CC ECO:0000269|PubMed:28526842, ECO:0000269|PubMed:29138484,
CC ECO:0000269|PubMed:3010044, ECO:0000269|PubMed:3023382,
CC ECO:0000269|PubMed:30524381, ECO:0000269|PubMed:3533941,
CC ECO:0000269|PubMed:3536870, ECO:0000269|PubMed:7592927,
CC ECO:0000269|PubMed:7934854}.
CC -!- ACTIVITY REGULATION: In the presence of 0.2 M NaCl, 2.0 mM sodium
CC cholate (bile salts) decreases expression from the ompC promoter; how
CC this is mediated is unknown. {ECO:0000269|PubMed:28423182}.
CC -!- SUBUNIT: Monomer in solution. Up to 8 OmpR molecules bind to the ompF
CC promoter; each 20 base pair (bp) region of the promoter binds 2
CC molecules of OmpR, which may only interact upon DNA-binding. Binds to
CC direct repeats in the 20 bp DNA fragments (PubMed:7592927). At pH 7.1
CC protein is monomeric, as the pH decreases to 6.5 and 6.1 about 70% is
CC dimeric, which is poorly phosphorylated. DNA-binding ability increases
CC at acidic pH (PubMed:29138484). {ECO:0000269|PubMed:29138484,
CC ECO:0000269|PubMed:7592927}.
CC -!- INTERACTION:
CC P0AA16; P0AEJ4: envZ; NbExp=2; IntAct=EBI-369514, EBI-1121750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3533941}.
CC -!- INDUCTION: 1.8-fold induced by growth in 15% sucrose, no change upon
CC growth at pH 5.6 (PubMed:30524381). Part of the ompR-envZ operon
CC (Probable). {ECO:0000269|PubMed:30524381, ECO:0000305|PubMed:2997120,
CC ECO:0000305|PubMed:6292199}.
CC -!- DOMAIN: Composed of an N-terminal response regulatory domain joined by
CC a flexible linker to the C-terminal DNA-binding domain; the relative
CC conformation of the 2 domains alters upon phosphorylation.
CC {ECO:0000269|PubMed:7568033}.
CC -!- PTM: Phosphorylated by EnvZ (PubMed:2656684, PubMed:2668281,
CC PubMed:2674113, PubMed:7934854, PubMed:2277041). Asp-55 is the primary
CC phosphate acceptor site, but Asp-11 may also serve as a phosphorylation
CC site, particularly in the absence of Asp-55 (PubMed:7934854)
CC (Probable). Phosphorylation stimulates the DNA-binding ability of OmpR
CC (PubMed:2674113). Dephosphorylated by EnvZ in the presence of ATP
CC (PubMed:2668281, PubMed:2558046, PubMed:7934854).
CC {ECO:0000269|PubMed:2277041, ECO:0000269|PubMed:2558046,
CC ECO:0000269|PubMed:2656684, ECO:0000269|PubMed:2668281,
CC ECO:0000269|PubMed:2674113, ECO:0000269|PubMed:7934854,
CC ECO:0000305|PubMed:2277041}.
CC -!- MASS SPECTROMETRY: Mass=27355; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7568033};
CC -!- MASS SPECTROMETRY: Mass=27438; Method=Electrospray; Note=The
CC (mono)phosphorylated form.; Evidence={ECO:0000269|PubMed:7568033};
CC -!- DISRUPTION PHENOTYPE: Loss of expression of OmpC and OmpF under low and
CC high osmolarity (PubMed:7934854). Deletion of both ompR and envZ leads
CC to loss of both OmpC and OmpF expression under 0% and 15% sucrose
CC (PubMed:2277041). Cells no longer reduce their internal pH in response
CC to external acid stress (PubMed:29138484). {ECO:0000269|PubMed:2277041,
CC ECO:0000269|PubMed:29138484, ECO:0000269|PubMed:7934854}.
CC -!- MISCELLANEOUS: Cross talk between this and the Che and Ntr two-
CC component systems can occur at least in vitro.
CC {ECO:0000269|PubMed:2558046}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.1; Type=Frameshift; Evidence={ECO:0000269|PubMed:2997120, ECO:0000269|PubMed:3010044};
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DR EMBL; J01656; AAA16241.1; -; Unassigned_RNA.
DR EMBL; U18997; AAA58202.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76430.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77886.1; -; Genomic_DNA.
DR PIR; H65135; RGECOR.
DR RefSeq; NP_417864.1; NC_000913.3.
DR RefSeq; WP_001157751.1; NZ_STEB01000004.1.
DR PDB; 1ODD; X-ray; 2.20 A; A=122-239.
DR PDB; 1OPC; X-ray; 1.95 A; A=130-239.
DR PDB; 2JPB; NMR; -; A=136-239.
DR PDB; 6LXL; X-ray; 3.56 A; A=136-239.
DR PDB; 6LXM; X-ray; 2.41 A; A/B/C=136-239.
DR PDB; 6LXN; X-ray; 2.93 A; A/B=136-239.
DR PDBsum; 1ODD; -.
DR PDBsum; 1OPC; -.
DR PDBsum; 2JPB; -.
DR PDBsum; 6LXL; -.
DR PDBsum; 6LXM; -.
DR PDBsum; 6LXN; -.
DR AlphaFoldDB; P0AA16; -.
DR SMR; P0AA16; -.
DR BioGRID; 4261267; 31.
DR BioGRID; 852222; 1.
DR DIP; DIP-31859N; -.
DR IntAct; P0AA16; 10.
DR STRING; 511145.b3405; -.
DR jPOST; P0AA16; -.
DR PaxDb; P0AA16; -.
DR PRIDE; P0AA16; -.
DR EnsemblBacteria; AAC76430; AAC76430; b3405.
DR EnsemblBacteria; BAE77886; BAE77886; BAE77886.
DR GeneID; 8912757; -.
DR GeneID; 947913; -.
DR KEGG; ecj:JW3368; -.
DR KEGG; eco:b3405; -.
DR PATRIC; fig|1411691.4.peg.3324; -.
DR EchoBASE; EB0666; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_6; -.
DR InParanoid; P0AA16; -.
DR OMA; NIHGEGF; -.
DR PhylomeDB; P0AA16; -.
DR BioCyc; EcoCyc:OMPR-MON; -.
DR EvolutionaryTrace; P0AA16; -.
DR PRO; PR:P0AA16; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000810; -.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoliWiki.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoliWiki.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoliWiki.
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 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome; Repressor; Stress response;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..239
FT /note="DNA-binding dual transcriptional regulator OmpR"
FT /id="PRO_0000081176"
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:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:7934854, ECO:0000305|PubMed:2277041"
FT MUTAGEN 11..12
FT /note="DD->AA: Loss of expression of OmpC and OmpF under
FT low and high osmolarity."
FT /evidence="ECO:0000269|PubMed:7934854"
FT MUTAGEN 11
FT /note="D->A: Reduced production of OmpF at low osmolarity,
FT reduced OmpC produced at high osmolarity. Significantly
FT decreased OmpR phosphorylation in vivo, no phosphorylation
FT in vitro. Loss of expression of OmpC and OmpF under low and
FT high osmolarity; when associated with A-55."
FT /evidence="ECO:0000269|PubMed:7934854"
FT MUTAGEN 12
FT /note="D->A: Wild-type production of OmpC and OmpF. No
FT production of OmpC at low osmolarity, incomplete repression
FT of OmpF, incomplete induction of OmpC at high osmolarity;
FT when associated with A-55."
FT /evidence="ECO:0000269|PubMed:7934854"
FT MUTAGEN 12
FT /note="D->V: Very poorly phosphorylated in vitro, produces
FT OmpF at 0% and 15% sucrose."
FT /evidence="ECO:0000269|PubMed:2277041"
FT MUTAGEN 15
FT /note="R->C: In ompR3; OmpF-, OmpC constitutive. Poorly
FT dephosphorylated by EnvZ."
FT /evidence="ECO:0000269|PubMed:2668281,
FT ECO:0000269|PubMed:3010044"
FT MUTAGEN 16
FT /note="L->Q: In ompR77; suppresses the OmpF- OmpC
FT constitutive phenotype of envZ11, has no phenotype alone."
FT /evidence="ECO:0000269|PubMed:3536870"
FT MUTAGEN 55
FT /note="D->A: Reduced production of OmpF at low osmolarity,
FT greatly reduced OmpC produced at high osmolarity.
FT Significantly decreased OmpR phosphorylation in vivo, no
FT phosphorylation in vitro. Loss of expression of OmpC and
FT OmpF under low and high osmolarity; when associated with A-
FT 11. No production of OmpC at low osmolarity, incomplete
FT repression of OmpF, incomplete induction of OmpC at high
FT osmolarity; when associated with A-12."
FT /evidence="ECO:0000269|PubMed:7934854"
FT MUTAGEN 55
FT /note="D->Q: Not phosphorylated in vitro, no OmpC or OmpF
FT under any growth conditions."
FT /evidence="ECO:0000269|PubMed:2277041"
FT MUTAGEN 71
FT /note="R->C: In ompR4; OmpC expressed at low levels even in
FT low osmolarity."
FT /evidence="ECO:0000269|PubMed:3010044"
FT MUTAGEN 150
FT /note="R->C: In ompR20; no OmpF expression, OmpC abnormally
FT expressed at high osmlolarity."
FT /evidence="ECO:0000269|PubMed:3010044"
FT MUTAGEN 164..182
FT /note="Missing: In ompR1; OmpF- OmpC- phenotype."
FT /evidence="ECO:0000269|PubMed:3010044"
FT MUTAGEN 203
FT /note="V->M: In ompR2; OmpF+ constitutive, OmpC-."
FT /evidence="ECO:0000269|PubMed:3010044"
FT MUTAGEN 207
FT /note="R->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:18195018"
FT MUTAGEN 209
FT /note="R->A: Loss of transcription activation."
FT /evidence="ECO:0000269|PubMed:18195018"
FT MUTAGEN 224
FT /note="T->C: Loss of transcription activation, loss of DNA-
FT binding, about 10% phosphorylation in vitro."
FT /evidence="ECO:0000269|PubMed:18195018"
FT MUTAGEN 225
FT /note="V->C: Wild-type transcription activation, decreased
FT DNA-binding, about 40% phosphorylation in vitro."
FT /evidence="ECO:0000269|PubMed:18195018"
FT MUTAGEN 226
FT /note="W->A,C: Loss of transcription activation, loss of
FT DNA-binding, about 20% phosphorylation in vitro."
FT /evidence="ECO:0000269|PubMed:18195018"
FT CONFLICT 7
FT /note="I -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1OPC"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1OPC"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:1OPC"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1OPC"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1OPC"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:1OPC"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:1OPC"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1OPC"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:1OPC"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6LXN"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:1OPC"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1OPC"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1OPC"
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
