Cloning and nucleotide sequence of the signal peptidase II (lsp)-gene from Staphylococcus carnosus

FEMS Microbiol Lett. 1995 Mar 1;126(3):233-9. doi: 10.1111/j.1574-6968.1995.tb07424.x.

Abstract

Staphylococcus carnosus TM300 is able to synthesize at least seven lipoproteins with molecular masses between 15 and 45 kDa; the proteins are located in the membrane fraction. It can be concluded that this strain 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 Staphylococcus 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 Pseudomonas 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. carnosus exhibited an increased globomycin resistance.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aspartic Acid Endopeptidases / chemistry
  • Aspartic Acid Endopeptidases / genetics*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Base Sequence
  • Chromosome Mapping
  • Chromosomes, Bacterial
  • Cloning, Molecular
  • Consensus Sequence
  • DNA, Bacterial / genetics
  • Enterobacter / chemistry
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Pseudomonas fluorescens / chemistry
  • Sequence Alignment
  • Staphylococcus / enzymology
  • Staphylococcus / genetics*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Aspartic Acid Endopeptidases
  • signal peptidase II

Associated data

  • GENBANK/X78084