{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0C079","secondaryAccessions":["P07007"],"uniProtkbId":"RELB_ECOLI","entryAudit":{"firstPublicDate":"1988-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1988-04-01","entryVersion":143,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9767574"}],"value":"Antitoxin RelB"}}},"genes":[{"geneName":{"value":"relB"},"orderedLocusNames":[{"value":"b1564"},{"value":"JW1556"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274135"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11717402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12123459"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18501926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18532983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19707553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22210768"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22981948"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9767574"}],"value":"Antitoxin component of a type II toxin-antitoxin (TA) system. 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"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19707553"}],"value":"Seems to be a principal mediator of cell death in liquid media"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11274135"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18501926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18532983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19297318"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22981948"}],"value":"Homotetramer formed by dimerization of dimers in solution (PubMed:18501926, PubMed:19747491). Forms an RelB(2)-RelE(2) 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:19747491, PubMed:22981948)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0C079","intActId":"EBI-1124503"},"interactantTwo":{"uniProtKBAccession":"P0C077","geneName":"relE","intActId":"EBI-549378"},"numberOfExperiments":3,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11717402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18501926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18532983"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22981948"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23432955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2990907"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9767574"}],"value":"By amino acid starvation, by glucose starvation and by chloramphenicol; induction is independent of ppGpp. Autorepressed by RelB, RelE acts as a corepressor (PubMed:18501926, PubMed:19747491, PubMed:22981948, PubMed:9767574). 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)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18501926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18532983"}],"value":"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)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11717402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"}],"value":"Probably degraded by Lon protease during amino acid starvation (PubMed:11717402). Degraded in vitro by Lon (PubMed:19747491)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11717402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19707553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20005847"}],"value":"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)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2990907"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"}],"value":"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"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the RelB/DinJ antitoxin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Antitoxin RelB","featureId":"PRO_0000097243"},{"type":"Mutagenesis","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":7,"modifier":"EXACT"}},"description":"Loss of DNA binding, 100-fold derepression of operon, still binds RelE.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18501926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"43-fold derepression of operon, partial loss of DNA-binding, still binds RelE.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"}],"alternativeSequence":{"originalSequence":"I","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"83-fold derepression of operon, loss of DNA-binding, still binds RelE.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"100-fold derepression of operon, loss of DNA-binding, still binds RelE.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19747491"}],"alternativeSequence":{"originalSequence":"S","alternativeSequences":["L","R"]}},{"type":"Mutagenesis","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"In relB101; 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