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P0AA16

- OMPR_ECOLI

UniProt

P0AA16 - OMPR_ECOLI

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Protein

Transcriptional regulatory protein OmpR

Gene

ompR

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

The N-terminus of this protein is required for the transcriptional expression of both major outer membrane protein genes ompF and ompC; its C-terminal moiety mediates the multimerization of the OmpR protein. As a multimer, it turns on the expression of the ompC gene; as a monomer, it turns on the expression of the ompF gene.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. phosphorelay response regulator activity Source: EcoliWiki

GO - Biological processi

  1. phosphorelay signal transduction system Source: EcoliWiki
  2. positive regulation of transcription, DNA-templated Source: EcoliWiki
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:OMPR-MONOMER.
ECOL316407:JW3368-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein OmpR
Gene namesi
Name:ompR
Synonyms:kmt, ompB
Ordered Locus Names:b3405, JW3368
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10672. ompR.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Transcriptional regulatory protein OmpRPRO_0000081176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 5514-aspartylphosphate1 PublicationPROSITE-ProRule annotation

Post-translational modificationi

Phosphorylated by EnvZ. Asp-55 is the primary phosphate acceptor site, but Asp-11 may also serve as a phosphorylation site, particularly in the absence of Asp-55.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AA16.
PRIDEiP0AA16.

Expressioni

Gene expression databases

GenevestigatoriP0AA16.

Interactioni

Subunit structurei

Monomer and multimer.

Protein-protein interaction databases

DIPiDIP-31859N.
IntActiP0AA16. 10 interactions.
STRINGi511145.b3405.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi138 – 1403
Beta strandi143 – 1464
Turni147 – 1504
Beta strandi151 – 1544
Beta strandi157 – 1593
Helixi163 – 17412
Helixi182 – 1898
Beta strandi192 – 1943
Helixi201 – 21212
Beta strandi220 – 2256
Turni226 – 2283
Beta strandi229 – 2324

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ODDX-ray2.20A122-239[»]
1OPCX-ray1.95A130-239[»]
2JPBNMR-A136-239[»]
ProteinModelPortaliP0AA16.
SMRiP0AA16. Positions 4-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA16.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 120120Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0745.
HOGENOMiHOG000034819.
InParanoidiP0AA16.
KOiK07659.
OMAiLRNANNM.
OrthoDBiEOG6G4VQG.
PhylomeDBiP0AA16.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR001867. Sig_transdc_resp-reg_C.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view]
SUPFAMiSSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA16-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQENYKILVV DDDMRLRALL ERYLTEQGFQ VRSVANAEQM DRLLTRESFH
60 70 80 90 100
LMVLDLMLPG EDGLSICRRL RSQSNPMPII MVTAKGEEVD RIVGLEIGAD
110 120 130 140 150
DYIPKPFNPR ELLARIRAVL RRQANELPGA PSQEEAVIAF GKFKLNLGTR
160 170 180 190 200
EMFREDEPMP LTSGEFAVLK ALVSHPREPL SRDKLMNLAR GREYSAMERS
210 220 230
IDVQISRLRR MVEEDPAHPR YIQTVWGLGY VFVPDGSKA
Length:239
Mass (Da):27,354
Last modified:September 13, 2005 - v1
Checksum:i823CA7720E9A1D2A
GO

Sequence cautioni

The sequence described in 1 Publication differs from that shown. Reason: Frameshift at position 210.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71I → N(PubMed:3010044)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01656 Unassigned RNA. Translation: AAA16241.1.
U18997 Genomic DNA. Translation: AAA58202.1.
U00096 Genomic DNA. Translation: AAC76430.1.
AP009048 Genomic DNA. Translation: BAE77886.1.
PIRiH65135. RGECOR.
RefSeqiNP_417864.1. NC_000913.3.
YP_492027.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76430; AAC76430; b3405.
BAE77886; BAE77886; BAE77886.
GeneIDi12932273.
947913.
KEGGiecj:Y75_p3771.
eco:b3405.
PATRICi32122246. VBIEscCol129921_3500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01656 Unassigned RNA. Translation: AAA16241.1 .
U18997 Genomic DNA. Translation: AAA58202.1 .
U00096 Genomic DNA. Translation: AAC76430.1 .
AP009048 Genomic DNA. Translation: BAE77886.1 .
PIRi H65135. RGECOR.
RefSeqi NP_417864.1. NC_000913.3.
YP_492027.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ODD X-ray 2.20 A 122-239 [» ]
1OPC X-ray 1.95 A 130-239 [» ]
2JPB NMR - A 136-239 [» ]
ProteinModelPortali P0AA16.
SMRi P0AA16. Positions 4-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31859N.
IntActi P0AA16. 10 interactions.
STRINGi 511145.b3405.

Proteomic databases

PaxDbi P0AA16.
PRIDEi P0AA16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76430 ; AAC76430 ; b3405 .
BAE77886 ; BAE77886 ; BAE77886 .
GeneIDi 12932273.
947913.
KEGGi ecj:Y75_p3771.
eco:b3405.
PATRICi 32122246. VBIEscCol129921_3500.

Organism-specific databases

EchoBASEi EB0666.
EcoGenei EG10672. ompR.

Phylogenomic databases

eggNOGi COG0745.
HOGENOMi HOG000034819.
InParanoidi P0AA16.
KOi K07659.
OMAi LRNANNM.
OrthoDBi EOG6G4VQG.
PhylomeDBi P0AA16.

Enzyme and pathway databases

BioCyci EcoCyc:OMPR-MONOMER.
ECOL316407:JW3368-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AA16.
PROi P0AA16.

Gene expression databases

Genevestigatori P0AA16.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR011006. CheY-like_superfamily.
IPR001867. Sig_transdc_resp-reg_C.
IPR016032. Sig_transdc_resp-reg_C-effctor.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view ]
SMARTi SM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46894. SSF46894. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Osmoregulation of gene expression. I. DNA sequence of the ompR gene of the ompB operon of Escherichia coli and characterization of its gene product."
    Wurtzel E.T., Chou M.-Y., Inouye M.
    J. Biol. Chem. 257:13685-13691(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular analysis of mutant ompR genes exhibiting different phenotypes as to osmoregulation of the ompF and ompC genes of Escherichia coli."
    Nara F., Matsuyama S., Mizuno T., Mizushima S.
    Mol. Gen. Genet. 202:194-199(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Primary characterization of the protein products of the Escherichia coli ompB locus: structure and regulation of synthesis of the OmpR and EnvZ proteins."
    Comeau D.E., Ikenaka K., Tsung K., Inouye M.
    J. Bacteriol. 164:578-584(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coli."
    Delgado J., Forst S., Harlocker S., Inouye M.
    Mol. Microbiol. 10:1037-1047(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT ASP-55.
  7. "Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site."
    Kondo H., Nakagawa A., Nishihira J., Nishimura Y., Mizuno T., Tanaka I.
    Nat. Struct. Biol. 4:28-31(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 136-235.
  8. "The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor."
    Martinez-Hackert E., Stock A.M.
    Structure 5:109-124(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 137-235.

Entry informationi

Entry nameiOMPR_ECOLI
AccessioniPrimary (citable) accession number: P0AA16
Secondary accession number(s): O31133
, P03025, P08981, P41405, Q2M770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2005
Last modified: October 29, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3