The gene encoding penicillin-binding protein 7, a homologue of the gene encoding a -endopeptidase, was cloned and sequenced. was located immediately downstream of the phenylalanine hydroxylase () operon. DNA sequencing revealed an open reading frame of 936 bp (starting with a GTG codon) which encodes a protein of 34115 Da. N-terminal amino acid sequencing confirmed the presence of a cleavable N-terminal signal peptide of 23 amino acids. Verification that the protein is a penicillin-binding protein was directly demonstrated by labelling with l-labelled penicillin X. Inactivation of by interposon mutagenesis resulted in no obvious phenotypic changes, but when was overexpressed in using a T7 expression system, cell lysis resulted. PbpG resembled PbpG in being associated with the membrane fraction. Two additional members of the PbpG subfamily were identified in the database. PbpG shows 63% identity with penicillin-binding protein 7 (PbpG) and 60% identity with PbpG, but only 23% identity with PbpG. The PbpG subfamily and three other subfamilies constituting the low-molecular-mass PBP protein family were analysed by multiple alignment of 26 sequences. PbpG exhibited the consensus motifs of other penicillin-binding proteins. Ten anchor residues were identified that are conserved at the family level within the superfamily of serine-active-site penicillin-interacting proteins.


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