{"metadata":{"accession":"PF10093","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR016633","hierarchy":null,"name":{"name":"Elongation-Factor P (EF-P) rhamnosyltransferase EarP","short":"EarP"},"description":[{"text":"<p>This entry includes family members such as EarP enzymes which are essential for post-translational activation of elongation factor P(EF-P). It was identified as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-beta-L-rhamnose as donor substrate [[cite:PUB00091040]]. This was further confirmed for Pseudomonas aeruginosa [[cite:PUB00091041]], Pseudomonas putida [[cite:PUB00091042]] and Neisseria meningitidis [[cite:PUB00091043]]. As for S. oneidensis [[cite:PUB00091044]] and P. aeruginosa [[cite:PUB00091045]], EarP enzyme acts as an inverting glycosyltransferase, thus mediating the formation of an alpha-L-rhamnosidic linkage. Structural analysis show that EarP is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B) and provide basis for arginine glycosylation by EarP [[cite:PUB00091042]]. Mutational analysis of efp and earP genes, resulted in a substantial decrease in the production of rhamnolipids and pyocyanin (important factors for colonization and invasion during infection) of P. aeruginosa. Collectively this indicates that EarP and EF-P are essential for P. aeruginosa pathogenicity [[cite:PUB00091040]].The protein family is also annotated in the CaZy Database as GT104.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00091042":{"PMID":28951478,"ISBN":null,"volume":"8","issue":"5","year":2017,"title":"Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.","URL":null,"raw_pages":null,"medline_journal":"MBio","ISO_journal":"MBio","authors":["Krafczyk R","Macosek J","Jagtap PKA","Gast D","Wunder S","Mitra P","Jha AK","Rohr J","Hoffmann-Roder A","Jung K","Hennig J","Lassak J."],"DOI_URL":"https://doi.org/10.1128/mBio.01412-17"},"PUB00091040":{"PMID":25686373,"ISBN":null,"volume":"11","issue":"4","year":2015,"title":"Arginine-rhamnosylation as new strategy to activate translation elongation factor P.","URL":null,"raw_pages":"266-70","medline_journal":"Nat Chem Biol","ISO_journal":"Nat. Chem. Biol.","authors":["Lassak J","Keilhauer EC","Furst M","Wuichet K","Godeke J","Starosta AL","Chen JM","Sogaard-Andersen L","Rohr J","Wilson DN","Haussler S","Mann M","Jung K."],"DOI_URL":"https://doi.org/10.1038/nchembio.1751"},"PUB00091045":{"PMID":28451332,"ISBN":null,"volume":"8","issue":"3","year":2017,"title":"Synthesis of rhamnosylated arginine glycopeptides and determination of the glycosidic linkage in bacterial elongation factor P.","URL":null,"raw_pages":"2296-2302","medline_journal":"Chem Sci","ISO_journal":"Chem Sci","authors":["Wang S","Corcilius L","Sharp PP","Rajkovic A","Ibba M","Parker BL","Payne RJ."],"DOI_URL":"https://doi.org/10.1039/c6sc03847f"},"PUB00091044":{"PMID":28451135,"ISBN":null,"volume":"7","issue":"12","year":2016,"title":"Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody.","URL":null,"raw_pages":"6995-7001","medline_journal":"Chem Sci","ISO_journal":"Chem Sci","authors":["Li X","Krafczyk R","Macosek J","Li YL","Zou Y","Simon B","Pan X","Wu QY","Yan F","Li S","Hennig J","Jung K","Lassak J","Hu HG."],"DOI_URL":"https://doi.org/10.1039/c6sc02889f"},"PUB00091043":{"PMID":26840407,"ISBN":null,"volume":"11","issue":"2","year":2016,"title":"Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability.","URL":null,"raw_pages":"e0147907","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Yanagisawa T","Takahashi H","Suzuki T","Masuda A","Dohmae N","Yokoyama S."],"DOI_URL":"https://doi.org/10.1371/journal.pone.0147907"},"PUB00091041":{"PMID":26060278,"ISBN":null,"volume":"6","issue":"3","year":2015,"title":"Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa.","URL":null,"raw_pages":"e00823","medline_journal":"MBio","ISO_journal":"MBio","authors":["Rajkovic A","Erickson S","Witzky A","Branson OE","Seo J","Gafken PR","Frietas MA","Whitelegge JP","Faull KF","Navarre W","Darwin AJ","Ibba M."],"DOI_URL":"https://doi.org/10.1128/mBio.00823-15"}},"set_info":{"accession":"CL0113","name":"GT-B"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":4,"interactions":0,"matches":1898,"pathways":0,"proteins":1864,"proteomes":1846,"sets":1,"structural_models":{"alphafold":1101},"structures":12,"taxa":2406},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":55,"alignment:full":821},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"5wxk","name":"EarP bound with domain I of EF-P"}}}