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P0C077

- RELE_ECOLI

UniProt

P0C077 - RELE_ECOLI

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Protein
mRNA interferase RelE
Gene
relE, b1563, JW1555
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Toxic component of a toxin-antitoxin (TA) module. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). 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. 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. Overexpression of RelE results in the inhibition of bacterial growth and a sharp decrease in colony-forming ability which is inhibited by the labile cognate antitoxin RelB. Overexpression also sharply increases persisters (cells that neither grow or die in presence of bactericidal agent and are largely responsible for high levels of biofilm tolerance to antimicrobials). Acts with RelB as a corepressor of relBE transcription.6 Publications
Seems to be a principal mediator of cell death in liquid media.6 Publications

GO - Molecular functioni

  1. endoribonuclease activity Source: EcoCyc
  2. protein binding Source: EcoCyc
  3. rRNA binding Source: UniProtKB-KW
  4. ribosome binding Source: EcoCyc

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  2. cellular response to amino acid starvation Source: EcoCyc
  3. mRNA catabolic process Source: EcoCyc
  4. negative regulation of translation Source: EcoCyc
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. response to antibiotic Source: EcoCyc
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Repressor, Toxin

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA interferase RelE (EC:3.1.-.-)
Alternative name(s):
Endoribonuclease RelE
Toxin RelE
Gene namesi
Name:relE
Ordered Locus Names:b1563, JW1555
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11131. relE.

Pathology & Biotechi

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611R → A: Greatly decreased mRNA cleavage. 1 Publication
Mutagenesisi81 – 833RER → AEA: Significant reduction in endonuclease activity, still binds RelB. 2 Publications
Mutagenesisi81 – 811R → A: Significantly decreased mRNA cleavage, significantly less translation inhibition which is countered by RelB. Almost complete loss of mRNA cleavage; when associated with F-87. 2 Publications
Mutagenesisi87 – 871Y → A: Significantly decreased mRNA cleavage. 1 Publication
Mutagenesisi87 – 871Y → F: No effect on mRNA cleavage, almost complete loss; when associated with A-81. 1 Publication
Mutagenesisi90 – 956AVKRIL → VTVTVT: Does not inhibit translation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9595mRNA interferase RelE
PRO_0000097245Add
BLAST

Proteomic databases

PaxDbiP0C077.
PRIDEiP0C077.

Expressioni

Inductioni

By amino acid starvation, by glucose starvation and by chloramphenicol. Induction is independent of ppGpp. Member of the relBE operon.1 Publication

Gene expression databases

GenevestigatoriP0C077.

Interactioni

Subunit structurei

Binds DNA as a RelE(2)-RelB2 heterotetramer. 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 inhibits its endonuclease activity.2 Publications

Protein-protein interaction databases

DIPiDIP-35978N.
IntActiP0C077. 11 interactions.
MINTiMINT-1282331.
STRINGi511145.b1563.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74
Helixi9 – 179
Helixi20 – 3516
Helixi40 – 423
Beta strandi45 – 473
Beta strandi50 – 545
Turni56 – 594
Beta strandi60 – 678
Helixi68 – 703
Beta strandi72 – 809
Helixi82 – 843
Helixi85 – 9410

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KC8NMR-A1-95[»]
2KC9NMR-A1-95[»]
3KIQX-ray3.30y1-95[»]
3KISX-ray3.30y1-95[»]
3KIUX-ray3.60y1-95[»]
3KIXX-ray3.60y1-95[»]
4FXEX-ray2.75D/E/F1-95[»]
4FXHX-ray2.40A/B1-95[»]
4FXIX-ray2.50A/B/C1-95[»]
ProteinModelPortaliP0C077.
SMRiP0C077. Positions 2-95.

Miscellaneous databases

EvolutionaryTraceiP0C077.

Family & Domainsi

Sequence similaritiesi

Belongs to the RelE toxin family.

Phylogenomic databases

eggNOGiCOG2026.
HOGENOMiHOG000219994.
KOiK06218.
OMAiGHADRYK.
OrthoDBiEOG6S52Q2.

Family and domain databases

InterProiIPR007712. RelE/ParE_toxin.
[Graphical view]
PfamiPF05016. Plasmid_stabil. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02385. RelE_StbE. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C077-1 [UniParc]FASTAAdd to Basket

« Hide

MAYFLDFDER ALKEWRKLGS TVREQLKKKL VEVLESPRIE ANKLRGMPDC   50
YKIKLRSSGY RLVYQVIDEK VVVFVISVGK RERSEVYSEA VKRIL 95
Length:95
Mass (Da):11,225
Last modified:April 1, 1988 - v1
Checksum:iF516B2E7A437CCEC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489827.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74636; AAC74636; b1563.
BAA15262; BAA15262; BAA15262.
GeneIDi12931249.
947549.
KEGGiecj:Y75_p1539.
eco:b1563.
PATRICi32118432. VBIEscCol129921_1636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02405 Genomic DNA. Translation: CAA26251.1 .
U00096 Genomic DNA. Translation: AAC74636.1 .
AP009048 Genomic DNA. Translation: BAA15262.1 .
PIRi B22830. QQECR1.
RefSeqi NP_416081.1. NC_000913.3.
YP_489827.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KC8 NMR - A 1-95 [» ]
2KC9 NMR - A 1-95 [» ]
3KIQ X-ray 3.30 y 1-95 [» ]
3KIS X-ray 3.30 y 1-95 [» ]
3KIU X-ray 3.60 y 1-95 [» ]
3KIX X-ray 3.60 y 1-95 [» ]
4FXE X-ray 2.75 D/E/F 1-95 [» ]
4FXH X-ray 2.40 A/B 1-95 [» ]
4FXI X-ray 2.50 A/B/C 1-95 [» ]
ProteinModelPortali P0C077.
SMRi P0C077. Positions 2-95.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35978N.
IntActi P0C077. 11 interactions.
MINTi MINT-1282331.
STRINGi 511145.b1563.

Proteomic databases

PaxDbi P0C077.
PRIDEi P0C077.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74636 ; AAC74636 ; b1563 .
BAA15262 ; BAA15262 ; BAA15262 .
GeneIDi 12931249.
947549.
KEGGi ecj:Y75_p1539.
eco:b1563.
PATRICi 32118432. VBIEscCol129921_1636.

Organism-specific databases

EchoBASEi EB1121.
EcoGenei EG11131. relE.

Phylogenomic databases

eggNOGi COG2026.
HOGENOMi HOG000219994.
KOi K06218.
OMAi GHADRYK.
OrthoDBi EOG6S52Q2.

Enzyme and pathway databases

BioCyci EcoCyc:EG11131-MONOMER.
ECOL316407:JW1555-MONOMER.
MetaCyc:EG11131-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0C077.
PROi P0C077.

Gene expression databases

Genevestigatori P0C077.

Family and domain databases

InterProi IPR007712. RelE/ParE_toxin.
[Graphical view ]
Pfami PF05016. Plasmid_stabil. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02385. RelE_StbE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene."
    Bech F.W., Joergensen S.T., Diderichsen B., Karlstroem O.H.
    EMBO J. 4:1059-1066(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / CS520.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family."
    Gotfredsen M., Gerdes K.
    Mol. Microbiol. 29:1065-1076(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TOXIN, FUNCTION AS A TRANSCRIPTIONAL COREPRESSOR.
  6. "Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes."
    Galvani C., Terry J., Ishiguro E.E.
    J. Bacteriol. 183:2700-2703(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, RIBOSOME-BINDING.
  7. "RelE, a global inhibitor of translation, is activated during nutritional stress."
    Christensen S.K., Mikkelsen M., Pedersen K., Gerdes K.
    Proc. Natl. Acad. Sci. U.S.A. 98:14328-14333(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TRANSLATION INHIBITOR, INDUCTION, DISRUPTION PHENOTYPE.
  8. "Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins."
    Pedersen K., Christensen S.K., Gerdes K.
    Mol. Microbiol. 45:501-510(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A TOXIN, MUTAGENESIS OF ARG-81 AND 90-ALA--LEU-95.
    Strain: K12.
  9. "The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site."
    Pedersen K., Zavialov A.V., Pavlov M.Y., Elf J., Gerdes K., Ehrenberg M.
    Cell 112:131-140(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ENDORIBONUCLEASE ON THE RIBOSOME.
  10. "Specialized persister cells and the mechanism of multidrug tolerance in Escherichia coli."
    Keren I., Shah D., Spoering A., Kaldalu N., Lewis K.
    J. Bacteriol. 186:8172-8180(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: RELATION WITH PERSISTERS.
  11. "A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation."
    Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.
    PLoS ONE 4:E6785-E6785(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL DEATH, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module."
    Li G.Y., Zhang Y., Inouye M., Ikura M.
    J. Mol. Biol. 380:107-119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  13. "mRNA interferases, sequence-specific endoribonucleases from the toxin-antitoxin systems."
    Yamaguchi Y., Inouye M.
    Prog. Mol. Biol. Transl. Sci. 85:467-500(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. "The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE."
    Neubauer C., Gao Y.G., Andersen K.R., Dunham C.M., Kelley A.C., Hentschel J., Gerdes K., Ramakrishnan V., Brodersen D.E.
    Cell 139:1084-1095(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN ISOLATION AND BOUND TO RIBOSOMES BEFORE AND AFTER MRNA CLEAVAGE, RIBOSOME-BINDING, RRNA-BINDING, MECHANISM OF CLEAVAGE, MUTAGENESIS OF ARG-61; ARG-81 AND TYR-87.
  15. "Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site."
    Li G.Y., Zhang Y., Inouye M., Ikura M.
    J. Biol. Chem. 284:14628-14636(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF MUTANT 81-ARG--ARG-83 IN COMPLEX WITH RELB FRAGMENT.

Entry informationi

Entry nameiRELE_ECOLI
AccessioniPrimary (citable) accession number: P0C077
Secondary accession number(s): P07008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 11, 2014
This is version 76 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

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