Control of synthesis and secretion of the Bacillus subtilis protein YqxM.

yqxM is a Bacillus subtilis gene of unknown function residing in an operon with sipW, which encodes a signal peptidase, and tasA, which encodes an antibiotic protein secreted in a sipW-dependent manner. YqxM was undetectable during growth in a variety of rich media, including Luria-Bertani (LB) medium, or in minimal media or under heat shock or ethanol stress conditions but was synthesized and secreted during growth in LB medium supplemented with 1.2 M NaCl. Consistent with the possible involvement of sipW in YqxM secretion, inactivation of sipW prevented YqxM secretion. YqxM was produced and secreted in a sipW-dependent manner during growth in LB medium when the sequences upstream of yqxM were replaced with those of the inducible P(spac) promoter. Coexpression of yqxM and sipW in Escherichia coli resulted in a decrease in the apparent molecular mass of YqxM, consistent with the removal of a signal peptide. These experiments suggest that YqxM production is induced by a high concentration of salt and that YqxM is secreted under the control of SipW. We hypothesize that during most conditions of growth, YqxM is present at very low levels or is not synthesized at all and that this low level or absence is due, at least in part, to posttranscriptional repression.