The twin arginine translocation system (Tat) is a protein secretion system that is conserved in bacteria, archaea, and plants. In Gram-negative bacteria, it is required for the export of folded proteins from the cytoplasm to the periplasm. There are 30 experimentally verified Tat substrates in Salmonella, including hydrogenase subunits, enzymes required for anaerobic respiration, and enzymes involved in peptidoglycan remodeling during cell division. Multiple studies have demonstrated the susceptibility of tat mutants to antimicrobial compounds such as SDS and bile; however, in this work we use growth curves and viable plate counts to demonstrate that cell wall targeting antibiotics (penicillins, carbapenems, cephalosporins, and fosfomycin) have increased killing against a Δtat strain. Further, we demonstrate that this increased killing is primarily due to defects in translocation of critical Tat substrates: MepK, AmiA, AmiC, and SufI. Finally, we show that a ΔhyaAB ΔhybABC ΔhydBC strain has an altered ΔΨ which impacts proper secretion of critical Tat substrates in aerobic growth conditions.
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