[en] 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.
De Meester F., Joris B., Lenzini M.V., Dehottay P., Erpicum T., Dusart J., Klein D., Ghuysen J.M., Frère J.M., Van Beeumen J. Biochem. J. 1987, 244:427-432.
Hopwood D.A., Bibb M.J., Chater K.F., Kieser T., Bruton C.J., Kieser H.M., Lydiate D.J., Smith C.P., Ward J.M., Schrempf H. Genetic manipulation of Streptomyces. A laboratory manual, The John Innes Foundation, Norwich, UK; 1985.
Katz E., Thompson C.J., Hopwood D.A. J. Gen. Microbiol. 1983, 129:2703-2714.
Johnson K., Dusart J., Campbell J.N., Ghuysen J.M. Antimicrob. Ag. Chemother. 1973, 3:289-298.
Westpheling J., Ranes M., Losick R. Nature (Lond.) 1985, 313:22-27.
Hopwood D.A., Bibb M.J., Chater K.F., Janssen G.R., Malpartida F., Smith C.P. Regulation of gene expression ‐ 25 years on , Booth, E. R., Higgins, C. F., eds, pp., Cambridge University Press, Cambridge, UK; 1986, 251-276.