{"metadata":{"accession":"PF06114","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010359","hierarchy":null,"name":{"name":"IrrE N-terminal-like domain","short":"Peptidase_M78"},"description":[{"text":"<p>This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif  from peptidase family M78. ImmA is encoded on a conjugative  transposon. Conjugating bacteria are able to transfer conjugative  transposons that can, for example, confer resistance to  antibiotics. The transposon is integrated into the chromosome, but  during conjugation excises itself and then moves to the recipient  bacterium and re-integrate into its chromosome. Typically a  conjugative tranposon encodes only the proteins required for this  activity and the proteins that regulate it. During exponential  growth, the ICEBs1 transposon of Bacillus subtilis is inactivated  by the immunity repressor protein ImmR, which is encoded by the  transposon and represses the genes for excision and transfer.  Cleavage of ImmR relaxes repression and allows transfer of the  transposon. ImmA has been shown to be essential for the cleavage  of ImmR [[cite:PUB00066798]]. This domain is also found in in metalloprotease IrrE, a central  regulator of DNA damage repair in Deinococcaceae [[cite:PUB00051490]], HTH-type transcriptional regulators RamB [[cite:PUB00074928]] and PrpC [[cite:PUB00074929]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00074928":{"PMID":15090522,"ISBN":null,"volume":"186","issue":"9","year":2004,"title":"RamB, a novel transcriptional regulator of genes involved in acetate metabolism of Corynebacterium glutamicum.","URL":null,"raw_pages":"2798-809","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Gerstmeir R","Cramer A","Dangel P","Schaffer S","Eikmanns BJ."],"DOI_URL":"http://dx.doi.org/10.1128/JB.186.9.2798-2809.2004"},"PUB00074929":{"PMID":22916289,"ISBN":null,"volume":"7","issue":"8","year":2012,"title":"A novel role of the PrpR as a transcription factor involved in the regulation of methylcitrate pathway in Mycobacterium tuberculosis.","URL":null,"raw_pages":"e43651","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Masiewicz P","Brzostek A","Wolanski M","Dziadek J","Zakrzewska-Czerwinska J."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0043651"},"PUB00051490":{"PMID":19150362,"ISBN":null,"volume":"386","issue":"3","year":2009,"title":"Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae.","URL":null,"raw_pages":"704-16","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Vujicic-Zagar A","Dulermo R","Le Gorrec M","Vannier F","Servant P","Sommer S","de Groot A","Serre L."],"DOI_URL":"http://dx.doi.org/10.1016/j.jmb.2008.12.062"},"PUB00066798":{"PMID":18761623,"ISBN":null,"volume":"70","issue":"3","year":2008,"title":"A conserved anti-repressor controls horizontal gene transfer by proteolysis.","URL":null,"raw_pages":"570-82","medline_journal":"Mol Microbiol","ISO_journal":"Mol. Microbiol.","authors":["Bose B","Auchtung JM","Lee CA","Grossman AD."],"DOI_URL":"http://dx.doi.org/10.1111/j.1365-2958.2008.06414.x"}},"set_info":{"accession":"CL0126","name":"Peptidase_MA"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":143,"interactions":0,"matches":21261,"pathways":0,"proteins":21240,"proteomes":11259,"sets":1,"structural_models":{"alphafold":13293},"structures":10,"taxa":16625},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":46,"alignment:full":11129},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}