{"metadata":{"accession":"PF04221","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007337","hierarchy":null,"name":{"name":"RelB antitoxin","short":"RelB"},"description":[{"text":"<p>RelE and RelB form a toxin-antitoxin system. RelE represses translation, probably through binding ribosomes ([[cite:PUB00009906]], [[cite:PUB00009907]]). RelB stably binds RelE, presumably deactivating it.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00009907":{"PMID":12123459,"ISBN":null,"volume":"45","issue":"2","year":2002,"title":"Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins.","URL":null,"raw_pages":"501-10","medline_journal":"Mol Microbiol","ISO_journal":"Mol. Microbiol.","authors":["Pedersen K","Christensen SK","Gerdes K."],"DOI_URL":"http://dx.doi.org/10.1046/j.1365-2958.2002.03027.x"},"PUB00009906":{"PMID":11274135,"ISBN":null,"volume":"183","issue":"8","year":2001,"title":"Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes.","URL":null,"raw_pages":"2700-3","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Galvani C","Terry J","Ishiguro EE."],"DOI_URL":"http://dx.doi.org/10.1128/JB.183.8.2700-2703.2001"}},"set_info":{"accession":"CL0057","name":"Met_repress"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":14,"interactions":0,"matches":5146,"pathways":0,"proteins":5136,"proteomes":2954,"sets":1,"structural_models":{"alphafold":3438},"structures":6,"taxa":5105},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":4,"alignment:full":2514},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4q2u","name":"Crystal structure of the E. coli DinJ-YafQ toxin-antitoxin complex"}}}