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Entry version 118 (26 Feb. 2020)
Sequence version 1 (13 Sep. 2005)
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Protein

DNA-binding dual transcriptional regulator OmpR

Gene

ompR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (PubMed:3010044, PubMed:3536870). Plays a central role in both acid and osmotic stress responses (PubMed:28526842, PubMed:30524381). Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (PubMed:3533941, PubMed:3023382, PubMed:2557454, PubMed:2403550, PubMed:7592927). Involved in acid stress response; this requires EnvZ but not OmpR phosphorylation (PubMed:29138484). Phosphorylated by EnvZ; this stimulates OmpR's DNA-binding ability (PubMed:2656684, PubMed:2668281, PubMed:2668953, PubMed:2674113, PubMed:2558046, PubMed:7934854). Is also dephosphorylated by EnvZ (PubMed:2668281, PubMed:2558046, PubMed:7934854). A single OmpR protein can bind to DNA; OmpR dimers can form on the DNA in either direction, suggesting that interactions between the 2 DNA-binding domains are weak or absent (PubMed:18195018).17 Publications

Miscellaneous

Cross talk between this and the Che and Ntr two-component systems can occur at least in vitro.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

In the presence of 0.2 M NaCl, 2.0 mM sodium cholate (bile salts) decreases expression from the ompC promoter; how this is mediated is unknown.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi135 – 234OmpR/PhoB-typePROSITE-ProRule annotationAdd BLAST100

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processStress response, Transcription, Transcription regulation, Two-component regulatory system

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA-binding dual transcriptional regulator OmpRCurated
Alternative name(s):
Transcriptional regulatory protein OmpRCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ompR
Synonyms:kmt, ompB
Ordered Locus Names:b3405, JW3368
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of expression of OmpC and OmpF under low and high osmolarity (PubMed:7934854). Deletion of both ompR and envZ leads to loss of both OmpC and OmpF expression under 0% and 15% sucrose (PubMed:2277041). Cells no longer reduce their internal pH in response to external acid stress (PubMed:29138484).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi11 – 12DD → AA: Loss of expression of OmpC and OmpF under low and high osmolarity. 1 Publication2
Mutagenesisi11D → A: Reduced production of OmpF at low osmolarity, reduced OmpC produced at high osmolarity. Significantly decreased OmpR phosphorylation in vivo, no phosphorylation in vitro. Loss of expression of OmpC and OmpF under low and high osmolarity; when associated with A-55. 1 Publication1
Mutagenesisi12D → A: Wild-type production of OmpC and OmpF. No production of OmpC at low osmolarity, incomplete repression of OmpF, incomplete induction of OmpC at high osmolarity; when associated with A-55. 1 Publication1
Mutagenesisi12D → V: Very poorly phosphorylated in vitro, produces OmpF at 0% and 15% sucrose. 1 Publication1
Mutagenesisi15R → C in ompR3; OmpF-, OmpC constitutive. Poorly dephosphorylated by EnvZ. 2 Publications1
Mutagenesisi16L → Q in ompR77; suppresses the OmpF- OmpC constitutive phenotype of envZ11, has no phenotype alone. 1 Publication1
Mutagenesisi55D → A: Reduced production of OmpF at low osmolarity, greatly reduced OmpC produced at high osmolarity. Significantly decreased OmpR phosphorylation in vivo, no phosphorylation in vitro. Loss of expression of OmpC and OmpF under low and high osmolarity; when associated with A-11. No production of OmpC at low osmolarity, incomplete repression of OmpF, incomplete induction of OmpC at high osmolarity; when associated with A-12. 1 Publication1
Mutagenesisi55D → Q: Not phosphorylated in vitro, no OmpC or OmpF under any growth conditions. 1 Publication1
Mutagenesisi71R → C in ompR4; OmpC expressed at low levels even in low osmolarity. 1 Publication1
Mutagenesisi150R → C in ompR20; no OmpF expression, OmpC abnormally expressed at high osmlolarity. 1 Publication1
Mutagenesisi164 – 182Missing in ompR1; OmpF- OmpC- phenotype. 1 PublicationAdd BLAST19
Mutagenesisi203V → M in ompR2; OmpF+ constitutive, OmpC-. 1 Publication1
Mutagenesisi207R → A: Loss of transcription activation. 1 Publication1
Mutagenesisi209R → A: Loss of transcription activation. 1 Publication1
Mutagenesisi224T → C: Loss of transcription activation, loss of DNA-binding, about 10% phosphorylation in vitro. 1 Publication1
Mutagenesisi225V → C: Wild-type transcription activation, decreased DNA-binding, about 40% phosphorylation in vitro. 1 Publication1
Mutagenesisi226W → A or C: Loss of transcription activation, loss of DNA-binding, about 20% phosphorylation in vitro. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000811761 – 239DNA-binding dual transcriptional regulator OmpRAdd BLAST239

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei554-aspartylphosphatePROSITE-ProRule annotation1 Publication1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by EnvZ (PubMed:2656684, PubMed:2668281, PubMed:2674113, PubMed:7934854, PubMed:2277041). 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 (PubMed:7934854) (Probable). Phosphorylation stimulates the DNA-binding ability of OmpR (PubMed:2674113). Dephosphorylated by EnvZ in the presence of ATP (PubMed:2668281, PubMed:2558046, PubMed:7934854).1 Publication6 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0AA16

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AA16

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0AA16

PRoteomics IDEntifications database

More...
PRIDEi
P0AA16

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

1.8-fold induced by growth in 15% sucrose, no change upon growth at pH 5.6 (PubMed:30524381). Part of the ompR-envZ operon (Probable).2 Publications1 Publication

Gene expression databases

CollecTF database of bacterial transcription factor binding sites

More...
CollecTFi
EXPREG_00000810

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer in solution. Up to 8 OmpR molecules bind to the ompF promoter; each 20 base pair (bp) region of the promoter binds 2 molecules of OmpR, which may only interact upon DNA-binding. Binds to direct repeats in the 20 bp DNA fragments (PubMed:7592927). At pH 7.1 protein is monomeric, as the pH decreases to 6.5 and 6.1 about 70% is dimeric, which is poorly phosphorylated. DNA-binding ability increases at acidic pH (PubMed:29138484).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
P0AEJ42EBI-369514,EBI-1121750

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261267, 31 interactors
852222, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-31859N

Protein interaction database and analysis system

More...
IntActi
P0AA16, 10 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3405

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0AA16

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AA16

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini6 – 120Response regulatoryPROSITE-ProRule annotationAdd BLAST115

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Composed of an N-terminal response regulatory domain joined by a flexible linker to the C-terminal DNA-binding domain; the relative conformation of the 2 domains alters upon phosphorylation.1 Publication

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000445_30_4_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AA16

KEGG Orthology (KO)

More...
KOi
K07659

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AA16

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00156 REC, 1 hit
cd00383 trans_reg_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011006 CheY-like_superfamily
IPR001867 OmpR/PhoB-type_DNA-bd
IPR016032 Sig_transdc_resp-reg_C-effctor
IPR001789 Sig_transdc_resp-reg_receiver
IPR039420 WalR-like
IPR036388 WH-like_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR26402 PTHR26402, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00072 Response_reg, 1 hit
PF00486 Trans_reg_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00448 REC, 1 hit
SM00862 Trans_reg_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46894 SSF46894, 1 hit
SSF52172 SSF52172, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51755 OMPR_PHOB, 1 hit
PS50110 RESPONSE_REGULATORY, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i823CA7720E9A1D2A
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence described in PubMed:6292199 differs from that shown. Reason: Frameshift.2 Publications

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti7I → N (PubMed:6292199).Curated1

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 27355 Da. Determined by ESI. 1 Publication
Molecular mass is 27438 Da. Determined by ESI. The (mono)phosphorylated form.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

Protein sequence database of the Protein Information Resource

More...
PIRi
H65135 RGECOR

NCBI Reference Sequences

More...
RefSeqi
NP_417864.1, NC_000913.3
WP_001157751.1, NZ_STEB01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76430; AAC76430; b3405
BAE77886; BAE77886; BAE77886

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8912757
947913

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3368
eco:b3405

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3324

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_001157751.1, NZ_STEB01000004.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ODDX-ray2.20A122-239[»]
1OPCX-ray1.95A130-239[»]
2JPBNMR-A136-239[»]
SMRiP0AA16
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261267, 31 interactors
852222, 1 interactor
DIPiDIP-31859N
IntActiP0AA16, 10 interactors
STRINGi511145.b3405

Proteomic databases

EPDiP0AA16
jPOSTiP0AA16
PaxDbiP0AA16
PRIDEiP0AA16

Genome annotation databases

EnsemblBacteriaiAAC76430; AAC76430; b3405
BAE77886; BAE77886; BAE77886
GeneIDi8912757
947913
KEGGiecj:JW3368
eco:b3405
PATRICifig|1411691.4.peg.3324

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0666

Phylogenomic databases

HOGENOMiCLU_000445_30_4_6
InParanoidiP0AA16
KOiK07659
PhylomeDBiP0AA16

Enzyme and pathway databases

BioCyciEcoCyc:OMPR-MONOMER
ECOL316407:JW3368-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AA16

Protein Ontology

More...
PROi
PR:P0AA16

Gene expression databases

CollecTFiEXPREG_00000810

Family and domain databases

CDDicd00156 REC, 1 hit
cd00383 trans_reg_C, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR011006 CheY-like_superfamily
IPR001867 OmpR/PhoB-type_DNA-bd
IPR016032 Sig_transdc_resp-reg_C-effctor
IPR001789 Sig_transdc_resp-reg_receiver
IPR039420 WalR-like
IPR036388 WH-like_DNA-bd_sf
PANTHERiPTHR26402 PTHR26402, 1 hit
PfamiView protein in Pfam
PF00072 Response_reg, 1 hit
PF00486 Trans_reg_C, 1 hit
SMARTiView protein in SMART
SM00448 REC, 1 hit
SM00862 Trans_reg_C, 1 hit
SUPFAMiSSF46894 SSF46894, 1 hit
SSF52172 SSF52172, 1 hit
PROSITEiView protein in PROSITE
PS51755 OMPR_PHOB, 1 hit
PS50110 RESPONSE_REGULATORY, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOMPR_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0AA16
Secondary accession number(s): O31133
, P03025, P08981, P41405, Q2M770
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2005
Last modified: February 26, 2020
This is version 118 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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