Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

PelA deacetylase activity is required for Pel polysaccharide synthesis in Pseudomonas aeruginosa.

Purified PelA hydrolyses p-nitrophenyl acetate; deacetylase active-site mutants lose activity, Pel production and Pel-dependent biofilm; PelA is in periplasmic and membrane fractions.

"We demonstrate that PelA exhibits deacetylase activity in vitro and identify four conserved residues in the putative active site required for this activity."

The RhlR quorum-sensing receptor controls Pseudomonas aeruginosa pathogenesis and biofilm development independently of its canonical homoserine lactone autoinducer.

Uses pelA deletions to test Pel dependence of RhlR colony biofilm phenotypes.

"We examined the colony biofilm phenotypes of the ΔpelA single and the ΔrhlRΔpelA and ΔrhlIΔpelA double mutants."

PMID:28972168

PelA and PelB proteins form a modification and secretion complex essential for Pel polysaccharide-dependent biofilm formation in Pseudomonas aeruginosa.

PelA binds the PelB TPR domain directly in the periplasm; the interaction raises deacetylase and lowers hydrolase activity.

"Copurification experiments indicated that the interaction between PelA and PelB is direct and that the deacetylase activity of PelA increases and its hydrolase activity decreases when these proteins interact."

PMID:40120681

Structural and functional analysis of Pseudomonas aeruginosa PelA provides insight into the modification of the Pel exopolysaccharide.

Crystal structure of PelA; the deacetylase domain founds CE21 and deacetylates alpha-1,4-GalNAc oligosaccharides; the hydrolase domain is an endo-alpha-1,4-N-acetylgalactosaminidase.

"Characterization of the deacetylase domain revealed that PelA is the founding member of a new carbohydrate esterase family, CE21."