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Entry version 110 (08 May 2019)
Sequence version 1 (01 Apr 1988)
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Protein

mRNA interferase toxin RelE

Gene

relE

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

Toxic component of a type II toxin-antitoxin (TA) system (PubMed:9767574). A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). In vitro acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. In vitro mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl-tRNA in the P site as well as on free 30S subunits (PubMed:12526800). In vivo cuts frequently in the first 100 codons, most frequently after the second and third base and rarely near the stop codon (PubMed:21324908). Overexpression of RelE results in the inhibition of bacterial growth and a sharp decrease in colony-forming ability which is neutralized by the labile cognate antitoxin RelB. Overexpression also sharply increases persisters (cells that neither grow nor die in the presence of bactericidal agents and are largely responsible for high levels of biofilm tolerance to antimicrobials) (PubMed:15576765). mRNA interferases play a role in bacterial persistence to antibiotics; overexpression of this protein induces persisters resistant to ciprofloxacin and ampicillin (PubMed:21788497). Plays a role in dormancy when expressed in high-density cells in the absence of antitoxin RelB; amino acid starvation and an unidentified extracellular factor promote dormancy, while expression of antitoxin RelB restores cell culturability (PubMed:22210768). Acts with RelB as a corepressor of relBE transcription, considerably increasing the repression of RelB alone. 2 RelB dimers bind to 2 operator sequences; DNA-binding and repression is stronger when complexed with toxin/corepressor RelE by conditional cooperativity (PubMed:9767574, PubMed:19747491, PubMed:18501926, PubMed:22981948).15 Publications
Seems to be a principal mediator of cell death in liquid media (PubMed:19707553). Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847).2 Publications
Cross-talk can occur between different TA systems. Ectopic expression of this toxin induces transcription of 7 tested TA systems (dinJ/yafQ, hicAB, mazEF, mqsRA, prlF(sohA)/yhaV, relBEF and yefM/yoeB) with specific cleavage of the relBEF mRNA produced immediately upstream and within the relB coding sequence. The cleaved mRNA can be translated into RelE, leading to a positive feedback cycle of RelE expression. The relBEF operon is required for transcription of the mazEF TA system operon during amino acid starvation.1 Publication

Miscellaneous

There are estimated to be 550-1100 RelB and 50-100 RelE molecules in rapidly growing cells of MG1655; as they have quite high affinity for each other (dissociation constant of 0.33 nM) there is probably less than 1 free RelE molecule per cell. The RelB2-RelE complex has a half-life of over 70 minutes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei52Proton acceptor1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei54Transition state stabilizer1 Publication1
Sitei61Transition state stabilizer1 Publication1
Active sitei81Proton donor1 Publication1

<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 functionEndonuclease, Hydrolase, Nuclease, Repressor, RNA-binding, rRNA-binding
Biological processAntibiotic resistance, Stress response, Toxin-antitoxin system, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11131-MONOMER
ECOL316407:JW1555-MONOMER
MetaCyc:EG11131-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_and_taxonomy_section">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:
mRNA interferase toxin RelE (EC:3.1.-.-)
Alternative name(s):
Endoribonuclease RelE
Toxin RelE
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:relE
Ordered Locus Names:b1563, JW1555
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG11131 relE

<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

GO - Cellular componenti

<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

Cells missing relBE have a higher steady-state level of translation during amino acid starvation than wild-type cells. They survive antibiotic treatment in log phase better than wild-type cells. Cells missing mazE-mazF survive hydroxyurea treatment better than wild-type; further disruption of relE-relB and tonB yields even better survival (PubMed:20005847). mRNA interferases play a role in bacterial persistence to antibiotics; as 10 mRNA interferases are successively deleted reduced levels of persisters are generated (PubMed:21788497).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi52K → A: Reduces mRNA cleavage rate constant 2100-fold. Reduces mRNA cleavage rate constant 1000000-fold; when associated with F-87. 1 Publication1
Mutagenesisi54K → A: Reduces mRNA cleavage rate constant 2700-fold. 1 Publication1
Mutagenesisi61R → A: Reduces mRNA cleavage rate constant 2700000-fold. 2 Publications1
Mutagenesisi81 – 83RER → AEA: Significant reduction in endonuclease activity, still binds RelB. 1 Publication3
Mutagenesisi81R → A: Reduces mRNA cleavage rate constant 60000-fold, significantly less translation inhibition which is countered by RelB. Almost complete loss of mRNA cleavage; when associated with F-87. 3 Publications1
Mutagenesisi87Y → A: Reduces mRNA cleavage rate constant 180000-fold. 2 Publications1
Mutagenesisi87Y → F: Reduces mRNA cleavage rate constant 130-fold. Almost complete loss of mRNA cleavage; when associated with A-81 (Ref.20). Reduces mRNA cleavage rate constant 1000000-fold; when associated with A-52 (Ref.18). 2 Publications1
Mutagenesisi90 – 95AVKRIL → VTVTVT: Does not inhibit translation. 1 Publication6

<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_00000972451 – 95mRNA interferase toxin RelEAdd BLAST95

Proteomic databases

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

More...
PaxDbi
P0C077

PRoteomics IDEntifications database

More...
PRIDEi
P0C077

<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

By amino acid starvation, by glucose starvation and by chloramphenicol; induction is independent of ppGpp. Autorepressed by RelB, RelE acts as a corepressor (PubMed:9767574, PubMed:19747491, PubMed:18501926, PubMed:22981948). Member of the relBEF operon (PubMed:2990907). Operon induced by ectopic expression of toxins HicA, HipA, MazF, MqsR and itself, but not by YafQ (PubMed:23432955).8 Publications

Gene expression databases

CollecTF database of bacterial transcription factor binding sites

More...
CollecTFi
EXPREG_00000890

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms an RelB2-RelE2 heterotetramer (PubMed:18501926, PubMed:22981948). Also forms an RelB2-RelE heterotrimer (PubMed:18532983, PubMed:19747491). The RelB2-RelE complex is probably the one that binds DNA and represses transcription, possibly as 2 heterotrimers, 1 bound to each of 2 operators (PubMed:22981948, PubMed:19747491). RelE occupies the A site of the 70S ribosome, making extensive contacts with the 16S rRNA. Its presence blocks access of tRNAs and translation factors. RelB bound to RelE prevents RelE from entering the ribosomal A site and thus inhibits its endonuclease activity (PubMed:19297318).6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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
relBP0C0793EBI-549378,EBI-1124503

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260243, 139 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1081 RelBE toxin-antitoxin complex

Database of interacting proteins

More...
DIPi
DIP-35978N

Protein interaction database and analysis system

More...
IntActi
P0C077, 12 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1563

<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

195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KC8NMR-A1-95[»]
2KC9NMR-A1-95[»]
4FXEX-ray2.75D/E/F1-95[»]
4FXHX-ray2.40A/B1-95[»]
4FXIX-ray1.80A/B/C1-95[»]
4V7JX-ray3.30Ay/By1-95[»]
4V7KX-ray3.60Ay/By1-95[»]

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

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SMRi
P0C077

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0C077

<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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RelE toxin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105K4U Bacteria
COG2026 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000219994

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0C077

KEGG Orthology (KO)

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KOi
K06218

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.2310.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007712 RelE/ParE_toxin
IPR035093 RelE/ParE_toxin_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05016 ParE_toxin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF143011 SSF143011, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02385 RelE_StbE, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P0C077-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAYFLDFDER ALKEWRKLGS TVREQLKKKL VEVLESPRIE ANKLRGMPDC
60 70 80 90
YKIKLRSSGY RLVYQVIDEK VVVFVISVGK RERSEVYSEA VKRIL
Length:95
Mass (Da):11,225
Last modified:April 1, 1988 - 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:iF516B2E7A437CCEC
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X02405 Genomic DNA Translation: CAA26251.1
U00096 Genomic DNA Translation: AAC74636.1
AP009048 Genomic DNA Translation: BAA15262.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B22830 QQECR1

NCBI Reference Sequences

More...
RefSeqi
NP_416081.1, NC_000913.3
WP_000323025.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74636; AAC74636; b1563
BAA15262; BAA15262; BAA15262

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29376887
947549

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1555
eco:b1563

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.699

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
X02405 Genomic DNA Translation: CAA26251.1
U00096 Genomic DNA Translation: AAC74636.1
AP009048 Genomic DNA Translation: BAA15262.1
PIRiB22830 QQECR1
RefSeqiNP_416081.1, NC_000913.3
WP_000323025.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KC8NMR-A1-95[»]
2KC9NMR-A1-95[»]
4FXEX-ray2.75D/E/F1-95[»]
4FXHX-ray2.40A/B1-95[»]
4FXIX-ray1.80A/B/C1-95[»]
4V7JX-ray3.30Ay/By1-95[»]
4V7KX-ray3.60Ay/By1-95[»]
SMRiP0C077
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260243, 139 interactors
ComplexPortaliCPX-1081 RelBE toxin-antitoxin complex
DIPiDIP-35978N
IntActiP0C077, 12 interactors
STRINGi511145.b1563

Proteomic databases

PaxDbiP0C077
PRIDEiP0C077

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74636; AAC74636; b1563
BAA15262; BAA15262; BAA15262
GeneIDi29376887
947549
KEGGiecj:JW1555
eco:b1563
PATRICifig|1411691.4.peg.699

Organism-specific databases

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

More...
EchoBASEi
EB1121
EcoGeneiEG11131 relE

Phylogenomic databases

eggNOGiENOG4105K4U Bacteria
COG2026 LUCA
HOGENOMiHOG000219994
InParanoidiP0C077
KOiK06218

Enzyme and pathway databases

BioCyciEcoCyc:EG11131-MONOMER
ECOL316407:JW1555-MONOMER
MetaCyc:EG11131-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0C077

Protein Ontology

More...
PROi
PR:P0C077

Gene expression databases

CollecTFiEXPREG_00000890

Family and domain databases

Gene3Di3.30.2310.20, 1 hit
InterProiView protein in InterPro
IPR007712 RelE/ParE_toxin
IPR035093 RelE/ParE_toxin_dom_sf
PfamiView protein in Pfam
PF05016 ParE_toxin, 1 hit
SUPFAMiSSF143011 SSF143011, 1 hit
TIGRFAMsiTIGR02385 RelE_StbE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiRELE_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: P0C077
Secondary accession number(s): P07008
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 8, 2019
This is version 110 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, Complete proteome, Reference proteome

Documents

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