CLONING AND NUCLEOTIDE-SEQUENCE OF THE SIGNAL PEPTIDASE-II (LSP)-GENEFROM STAPHYLOCOCCUS-CARNOSUS

Staphylacoccus carnosus TM300 is able to synthesize at least seven lip oproteins with molecular masses between 15 and 45 kDa; the proteins ar e located in the membrane fraction. It can be concluded that this stra in also posesses the enzymes involved in lipoprotein modification and prolipoprotein signal peptidase (signal peptidase II) processing. The gene encoding the prolipoprotein signal peptidase, lsp, from Staphyloc occus carnosus TM300 was cloned in Escherichia coli and sequenced. The deduced amino acid sequence of the Lsp showed amino acid similarities with the Lsp's of S. aureus, Enterobacter aerogenes, E. coli, and Pse udomonas fluorescens. The hydropathy profile reveals four hydrophobic segments which are homologous to the putative transmembrane regions of the E. coli signal peptidase II. E. coli strains carrying lsp of S. c arnosus exhibited an increased globomycin resistance.