Elongation-Factor P (EF-P) rhamnosyltransferase EarP
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. This was further confirmed for Pseudomonas aeruginosa, Pseudomonas putida and Neisseria meningitidis. As for S. oneidensis and P. aeruginosa, 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. 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.The protein family is also annotated in the CaZy Database as GT104.
Jiyao W et al.(2023). "The conserved domain database in 2023.",