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Replicative DNA helicase DnaC in *Staphylococcus aureus* is the principal enzyme responsible for unwinding double-stranded DNA by translocating in the 3′–5′ direction ahead of the DNA replication machinery, using the energy of ATP hydrolysis. It is essential for both initiation and elongation steps of chromosome replication, ensuring proper DNA strand separation for polymerase access and replication fork progression. DnaC is highly conserved among bacteria and is an attractive antibacterial drug target due to its crucial role in bacterial survival and proliferation. There are no approved drugs directly targeting DnaC in clinical use, but its mechanism has spurred research into novel helicase inhibitors as new antibacterial agents. Important caveat: There are multiple DNA helicases in *S. aureus* (e.g., PcrA, PriA, DinG), but DnaC is regarded as the principal replicative helicase. Some proteins annotated as "helicase" (e.g., DinG in *S. aureus*) lack helicase activity and act instead as nucleases; thus, precise nomenclature and functional validation are important. All above information corresponds to the canonical replicative DNA helicase DnaC, not other *S. aureus* helicase-like proteins, unless otherwise specified.
Drugs (investigational) inhibiting DNA helicase would block ATP hydrolysis or DNA unwinding activity, preventing bacterial DNA replication and leading to cell death.
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