The carboxy terminal domain of Epr, a minor extracellular serine protease, is essential for the swarming motility of Bacillus subtilis 168

FEMS Microbiol Lett. 2006 Apr;257(1):24-31. doi: 10.1111/j.1574-6968.2006.00151.x.

Abstract

In this study we have investigated the role of Epr, a minor extracellular serine protease, in the swarming motility of Bacillus subtilis 168. We identified that the protease activity of Epr was dispensable for swarming. Since the protease activity of Epr was confined to its N-terminal domain, we hypothesized instead that its C-terminal domain (CTD) could be critical for swarming. Our study showed that not only the expression of Epr-CTD was necessary, but also its secretion was crucial for the swarming motility of B. subtilis 168.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / enzymology
  • Bacillus subtilis / genetics
  • Bacillus subtilis / physiology*
  • Gene Expression Regulation, Bacterial*
  • Movement
  • Mutagenesis, Site-Directed
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*

Substances

  • Epr serine proteinase
  • Serine Endopeptidases