Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor.
A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986) Gene 42, 31-36], was sequenced. The gene codes for a 314-amino-acid precursor, the N-terminal region of which has the characteristics of a signal peptide. The beta-lactamase as excreted by the host strain S. lividans PD6 has a ragged N-terminus, indicating either the presence of a leader peptidase of poor specificity or the action of an aminopeptidase. The primary structure (as deduced from the nucleotide sequence) was confirmed by amino acid sequencing of a 16-residue stretch at the amino terminus of the protein, a 12-residue stretch containing the active-site serine [De Meester et al. (1987) Biochem. J. 244, 427-432] and a 23-residue stretch obtained by trypsin digestion of the protein. The beta-lactamase belongs to class A, has three half-cystine residues (one of which occurs on the amino side of the active-site serine) and is inactivated by thiol reagents. Putative ribosome binding site and terminator region were identified.
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D004262:DNA Restriction Enzymes; D004792:Enzyme Precursors / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D010957:Plasmids; D011401:Promoter Regions, Genetic; D013302:Streptomyces / Q000201:enzymology / Q000235:genetics*; D013728:Terminator Regions, Genetic; D001618:beta-Lactamases / Q000235:genetics*
D004792:Enzyme Precursors; D004262:DNA Restriction Enzymes; D001618:beta-Lactamases