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Protein

Antitoxin RelB

Gene

relB

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

Functioni

Antitoxin component of a type II toxin-antitoxin (TA) module. Counteracts the effect of cognate toxin RelE via direct protein-protein interaction, preventing RelE from entering the ribosome A site and thus inhibiting its endoribonuclease activity. An autorepressor of relBE operon transcription. 2 RelB dimers bind to 2 operator sequences; DNA-binding and repression is stronger when complexed with toxin/corepressor RelE by conditional cooperativity (PubMed:18501926, PubMed:22981948). Increased transcription rate of relBE and activation of relE is consistent with a lower level of RelB in starved cells due to degradation of RelB by protease Lon.10 Publications
Seems to be a principal mediator of cell death in liquid media.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Stress response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10836-MONOMER.
ECOL316407:JW1556-MONOMER.
MetaCyc:EG10836-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin RelB1 Publication
Gene namesi
Name:relB
Ordered Locus Names:b1564, JW1556
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10836. relB.

Pathology & Biotechi

Disruption phenotypei

Essential, it cannot be deleted if a copy of relE remains in the cell. 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).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71R → A: Loss of DNA binding, 100-fold derepression of operon, still binds RelE. 2 Publications
Mutagenesisi8 – 81I → A: 43-fold derepression of operon, partial loss of DNA-binding, still binds RelE. 1 Publication
Mutagenesisi13 – 131K → A: 83-fold derepression of operon, loss of DNA-binding, still binds RelE. 1 Publication
Mutagenesisi28 – 281S → L or R: 100-fold derepression of operon, loss of DNA-binding, still binds RelE. 1 Publication
Mutagenesisi39 – 391A → T in relB101; a delayed relaxed phenotype. 1 Publication
Mutagenesisi45 – 451P → L in relB102; a delayed relaxed phenotype. 1 Publication
Mutagenesisi45 – 451P → T in relB35; a delayed relaxed phenotype. 1 Publication
Mutagenesisi66 – 7914Missing : Protein no longer tetramerizes. 1 PublicationAdd
BLAST
Mutagenesisi71 – 799Missing : Protein still tetramerizes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7979Antitoxin RelBPRO_0000097243Add
BLAST

Post-translational modificationi

Probably degraded by Lon protease during amino acid starvation (PubMed:11717402). Degraded in vitro by Lon (PubMed:19747491).2 Publications

Proteomic databases

PaxDbiP0C079.
PRIDEiP0C079.

Expressioni

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 RelE, but not by YafQ (PubMed:23432955).8 Publications

Gene expression databases

CollecTFiEXPREG_000008a0.

Interactioni

Subunit structurei

Homotetramer formed by dimerization of dimers in solution (PubMed:19747491, PubMed:18501926). Forms an RelB(2)-RelE2 heterotetramer (PubMed:18501926, PubMed:22981948). Also forms an RelB(2)-RelE heterotrimer (PubMed:18532983, PubMed:19747491). The RelB(2)-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).6 Publications

Protein-protein interaction databases

BioGridi4260244. 61 interactions.
DIPiDIP-48258N.
IntActiP0C079. 5 interactions.
STRINGi511145.b1564.

Structurei

Secondary structure

1
79
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi10 – 2314Combined sources
Helixi27 – 4115Combined sources
Helixi49 – 6719Combined sources
Beta strandi71 – 744Combined sources
Helixi76 – 783Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K29NMR-A/B1-50[»]
2KC8NMR-B47-79[»]
4FXEX-ray2.75A/B/C1-79[»]
ProteinModelPortaliP0C079.
SMRiP0C079. Positions 2-79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C079.

Family & Domainsi

Domaini

Dimerizes and binds DNA via its N-terminus (residues 1-50), binds toxin RelE via the C-terminus (residues 47-79) (PubMed:18501926, PubMed:18532983). Tetramerization probably requires amino acids between residues 66 and 71 (PubMed:18501926).2 Publications

Sequence similaritiesi

Belongs to the RelB/DinJ antitoxin family.Curated

Phylogenomic databases

eggNOGiCOG3077. LUCA.
HOGENOMiHOG000008424.
KOiK18918.
OMAiTINIRVN.
OrthoDBiEOG6K13ZM.

Family and domain databases

InterProiIPR007337. RelB/DinJ.
[Graphical view]
PfamiPF04221. RelB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02384. RelB_DinJ. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSINLRIDD ELKARSYAAL EKMGVTPSEA LRLMLEYIAD NERLPFKQTL
60 70
LSDEDAELVE IVKERLRNPK PVRVTLDEL
Length:79
Mass (Da):9,071
Last modified:April 1, 1988 - v1
Checksum:i3DD2107337226FAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02405 Genomic DNA. Translation: CAA26250.1.
U00096 Genomic DNA. Translation: AAC74637.1.
AP009048 Genomic DNA. Translation: BAA15263.1.
PIRiA22830. BVECRB.
RefSeqiNP_416082.1. NC_000913.3.
WP_000534858.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74637; AAC74637; b1564.
BAA15263; BAA15263; BAA15263.
GeneIDi948308.
KEGGiecj:JW1556.
eco:b1564.
PATRICi32118434. VBIEscCol129921_1637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02405 Genomic DNA. Translation: CAA26250.1.
U00096 Genomic DNA. Translation: AAC74637.1.
AP009048 Genomic DNA. Translation: BAA15263.1.
PIRiA22830. BVECRB.
RefSeqiNP_416082.1. NC_000913.3.
WP_000534858.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K29NMR-A/B1-50[»]
2KC8NMR-B47-79[»]
4FXEX-ray2.75A/B/C1-79[»]
ProteinModelPortaliP0C079.
SMRiP0C079. Positions 2-79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260244. 61 interactions.
DIPiDIP-48258N.
IntActiP0C079. 5 interactions.
STRINGi511145.b1564.

Proteomic databases

PaxDbiP0C079.
PRIDEiP0C079.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74637; AAC74637; b1564.
BAA15263; BAA15263; BAA15263.
GeneIDi948308.
KEGGiecj:JW1556.
eco:b1564.
PATRICi32118434. VBIEscCol129921_1637.

Organism-specific databases

EchoBASEiEB0829.
EcoGeneiEG10836. relB.

Phylogenomic databases

eggNOGiCOG3077. LUCA.
HOGENOMiHOG000008424.
KOiK18918.
OMAiTINIRVN.
OrthoDBiEOG6K13ZM.

Enzyme and pathway databases

BioCyciEcoCyc:EG10836-MONOMER.
ECOL316407:JW1556-MONOMER.
MetaCyc:EG10836-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0C079.
PROiP0C079.

Gene expression databases

CollecTFiEXPREG_000008a0.

Family and domain databases

InterProiIPR007337. RelB/DinJ.
[Graphical view]
PfamiPF04221. RelB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02384. RelB_DinJ. 1 hit.
ProtoNetiSearch...

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], OPERON, MUTAGENESIS OF ALA-39 AND PRO-45.
    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 AN ANTITOXIN, FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, INDUCTION.
  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, DNA-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, CLEAVAGE BY LON PROTEASE, 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 AN ANTITOXIN.
    Strain: K12.
  9. "Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity."
    Overgaard M., Borch J., Joergensen M.G., Gerdes K.
    Mol. Microbiol. 69:841-857(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DOMAIN, DNA-BINDING.
    Strain: K12.
  10. "RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB."
    Overgaard M., Borch J., Gerdes K.
    J. Mol. Biol. 394:183-196(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INDUCTION, CLEAVAGE BY LON PROTEASE, DNA-BINDING, MUTAGENESIS OF ARG-7; ILE-8; LYS-13 AND SER-28.
    Strain: K12.
  11. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "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.
  13. "RelE-mediated dormancy is enhanced at high cell density in Escherichia coli."
    Tashiro Y., Kawata K., Taniuchi A., Kakinuma K., May T., Okabe S.
    J. Bacteriol. 194:1169-1176(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  14. "Transcriptional cross-activation between toxin-antitoxin systems of Escherichia coli."
    Kasari V., Mets T., Tenson T., Kaldalu N.
    BMC Microbiol. 13:45-45(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY OTHER TA MODULES.
    Strain: K12 / BW25113.
  15. "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: STRUCTURE BY NMR OF 1-50, FUNCTION, DNA-BINDING, SUBUNIT, INDUCTION, DOMAINS, MUTAGENESIS OF ARG-7; 66-LEU--LEU-79 AND 71-PRO--LEU-79.
  16. "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 47-79 IN COMPLEX WITH RELE, SUBUNIT.
  17. "The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity."
    Boggild A., Sofos N., Andersen K.R., Feddersen A., Easter A.D., Passmore L.A., Brodersen D.E.
    Structure 20:1641-1648(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH RELB, FUNCTION, SUBUNIT, INDUCTION.

Entry informationi

Entry nameiRELB_ECOLI
AccessioniPrimary (citable) accession number: P0C079
Secondary accession number(s): P07007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 13, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

A number of site directed mutants give rise to a delayed relaxed phenotype; RNA synthesis resumes 10 minutes after amino acid starvation, an unusually slow recovery from periods of starvation, accumulation of a translation inhibitor.1 Publication
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 RelB(2)-RelE complex has a half-life of over 70 minutes.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.