Variability in the posttranslational processing of penicillin-binding protein 1b among different strains of Escherichia coli.
Screening of a number of unrelated strains of Escherichia coli confirms the existence of at least two patterns of molecular forms for penicillin-binding protein 1b in E. coli cell envelopes. Our data support that the beta-form of this protein is produced by posttranslational modification of the alpha-form and suggest that the absence of the beta-form in some strains is due to a strain-dependent variability in the alpha-form processing mechanism.
D000217:Acyltransferases / Q000235:genetics*; D001426:Bacterial Proteins; D002352:Carrier Proteins; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D006602:Hexosyltransferases / Q000235:genetics*; D009097:Multienzyme Complexes / Q000235:genetics*; D002267:Muramoylpentapeptide Carboxypeptidase; D046915:Penicillin-Binding Proteins; D010449:Peptide Mapping; D010458:Peptidyl Transferases / Q000235:genetics*; D010957:Plasmids; D011499:Protein Processing, Post-Translational; D013045:Species Specificity
D001426:Bacterial Proteins; D002352:Carrier Proteins; D009097:Multienzyme Complexes; D046915:Penicillin-Binding Proteins; D000217:Acyltransferases; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase