The ponA gene of Enterococcus faecalis JH2-2 codes for a low-affinity class A penicillin-binding protein.
A soluble derivative of the Enterococcus faecalis JH2-2 class A PBP1 (*PBP1) was overproduced and purified. It exhibited a glycosyltransferase activity on the Escherichia coli 14C-labeled lipid II precursor. As a DD- peptidase, it could hydrolyze thiolester substrates with efficiencies similar to those of other class A penicillin-binding proteins (PBPs) and bind beta-lactams, but with k2/K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs.
Duez
Colette
C
Centre d'Ingénierie des Protéines, Institut de Chimie, B6, Université de Liege, B-4000 Sart Tilman, Belgium. jcoyette@ulg.ac.be
Hallut
Séverine
S
Rhazi
Noureddine
N
Hubert
Séverine
S
Amoroso
Ana
A
Bouillenne
Fabrice
F
Piette
André
A
Coyette
Jacques
J
D000900:Anti-Bacterial Agents / Q000378:metabolism; D001426:Bacterial Proteins; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D013293:Enterococcus faecalis / Q000235:genetics*; D005798:Genes, Bacterial; D016695:Glycosyltransferases / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D046915:Penicillin-Binding Proteins
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D016695:Glycosyltransferases