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In the Gram-positive pathogen  Staphylococcus aureus , the membrane-bound ATP-dependent metalloprotease FtsH plays a critical role in resistance to various stressors. However, the molecular mechanism of the FtsH functions is not known. Here, we identified core FtsH target proteins in  S .  aureus . In the strains Newman and USA300, the abundance of 33 proteins were altered in both strains, of which 11 were identified as core FtsH substrate protein candidates. In the strain Newman and some other  S .  aureus  strains, the sensor histidine kinase SaeS has an L18P (T53C in  saeS ) substitution, which transformed the protein into an FtsH substrate. Due to the increase of SaeS L18P in the  ftsH  mutant, Eap, a  sae -regulon protein, was also increased in abundance, causing the Newman-specific cell-aggregation phenotype. Regardless of the strain background, however, the  ftsH  mutants showed lower virulence and survival in a murine infection model. Our study illustrates the elasticity of the bacterial regulatory network, which can be rewired by a single substitution mutation.

Rewiring of the FtsH regulatory network by a single nucleotide change in saeS of Staphylococcus aureus