The necessity of InvC for virulence and its conserved structure across several pathogen species makes it an attractive target for T3SS inhibition. InvC is also highly related to several other T3SS ATPases, like Shigella Spa47, Yersinia YscN, E. coli EscN, and Pseudomonas HrcN, sharing 38-75% of its sequence with these orthologs -giving it potential as a target for broad-spectrum activity. The dysfunctionality of ATPase-knockout mutants is not restricted to Salmonella; in E. coli, deletion of the EscN gene (an ortholog to InvC) renders the pathogen unable to develop or secrete virulence factors . Similarly, in Y. enterocolitica, deletion of the YscN gene (another ortholog to InvC) abolishes the secretion of bacterial effectors . In Salmonella, when InvC is heavily destabilized, mutant strains are defective for translocation of effectors, bacterial egress, cytosolic colonization, and vacuolar replication . In addition, inhibition of T3SS ATPase avoids the risk of cross-reaction between T3SS ATPase inhibitors and human ATPase enzymes because bacterial ATPase and human ATPase share less than 25% of their sequences and their active sites are structurally different . Though there are many existing inhibitors of Salmonella T3SS, none have been shown to target the InvC protein vital for combating antibacterial resistance .