Protein Family Models

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 [1]. This was further confirmed for Pseudomonas aeruginosa [2], Pseudomonas putida [3] and Neisseria meningitidis [4]. As for S. oneidensis [5] and P. aeruginosa [6], 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 [3]. 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 [1].The protein family is also annotated in the CaZy Database as GT104. [1]. 25686373. Arginine-rhamnosylation as new strategy to activate translation. elongation factor P.. 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;. Nat Chem Biol. 2015;11:266-270.. [2]. 26060278. Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic. Resistance in Pseudomonas aeruginosa.. Rajkovic A, Erickson S, Witzky A, Branson OE, Seo J, Gafken PR,. Frietas MA, Whitelegge JP, Faul. TRUNCATED at 1650 bytes (from Pfam)

Gene:

earP

Date:

2024-08-14

elongation factor P maturation arginine rhamnosyltransferase EarP rhamnosylates EF-P on arginine 32

Date:

2018-03-16

Translation elongation factor P (EF-P) is universal in bacteria. It alleviates stalling at stretches of polyproline. Several alternative post-translational modifications occur in different lineages, and in most cases are essential for viability. This HMM describes the EF-P arginine sidechain-modifying rhamnosyltransferase EarP. Other modifications include beta-lysylation in Escherichia coli, 5-aminopentanolylation in Bacillus subtilis, and a hypusine modification in the related elongation factor of archaea (aIF5A) or eukaryotes (eIF5A).

Gene:

earP

Date:

2024-08-05