v5.1.0.3
Cicer data from the Legume Information System
Description | 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. |
Namespace | Family |