{"metadata":{"accession":"PF04315","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR007411","hierarchy":null,"name":{"name":"Elongation factor P hydroxylase","short":"EpmC"},"description":[{"text":"<p>This family catalyses the final step in the elongation factor P modification pathway. It hydroxylates Lys-34 of elongation factor P [[cite:PUB00109139]].  Members of this family have a conserved HEXXH motif, suggesting they are putative peptidases of zincin fold [[cite:PUB00075429]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00075429":{"PMID":23671590,"ISBN":null,"volume":"8","issue":"5","year":2013,"title":"CLCAs - a family of metalloproteases of intriguing phylogenetic distribution and with cases of substituted catalytic sites.","URL":null,"raw_pages":"e62272","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Lenart A","Dudkiewicz M","Grynberg M","Pawlowski K."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0062272"},"PUB00109139":{"PMID":22706199,"ISBN":null,"volume":"8","issue":"8","year":2012,"title":"Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.","URL":null,"raw_pages":"695-7","medline_journal":"Nat Chem Biol","ISO_journal":"Nat Chem Biol","authors":["Peil L","Starosta AL","Virumae K","Atkinson GC","Tenson T","Remme J","Wilson DN."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":3,"interactions":0,"matches":1795,"pathways":0,"proteins":1795,"proteomes":1777,"sets":0,"structural_models":{"alphafold":1135},"structures":2,"taxa":2428},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":26,"alignment:full":607},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4pdn","name":"Crystal structure of E. coli YfcM"}}}