Virulence-related type III secretion systems are present in many Gram-negative bacterial pathogens. These complex devices
translocate proteins, called effectors, from the bacterium into the eukaryotic host cell. Here, we identify the product of srfJ, a
Salmonella enterica serovar Typhimurium gene regulated by SsrB, as a new substrate of the type III secretion system encoded by
Salmonella pathogenicity island 2. The N-terminal 20-amino-acid segment of SrfJ was recognized as a functional secretion and
translocation signal specific for this system. Transcription of srfJ was positively regulated by the PhoP/PhoQ system in an SsrBdependent
manner and was negatively regulated by the Rcs system in an SsrB-independent manner. A screen for regulators of an
srfJ-lacZ transcriptional fusion using the T-POP transposon identified IolR, the regulator of genes involved in myo-inositol utilization,
as an srfJ repressor. Our results suggest that SrfJ is synthesized both inside the host, in response to intracellular conditions,
and outside the host, in myo-inositol-rich environments
