Arsenical pump-driving ATPase (ArsA)

The Arsenical pump-driving ATPase, commonly known as ArsA, is a specialized enzyme in Escherichia coli that provides resistance to toxic metalloids like arsenite [As(III)] and antimonite [Sb(III)] (UniProt P08690). It serves as the catalytic subunit of the ArsAB efflux pump, where it hydrolyzes ATP to provide the energy necessary for the active transport of these toxins out of the cell (Rosen, 2002). ArsA is an allosterically regulated enzyme; its ATPase activity is significantly stimulated by the binding of its substrates, ensuring that energy is only expended when the toxins are present in the cytoplasm (Zhou et al., 2000). This protein is a member of the oxyanion-translocating ATPase family and is essential for bacterial survival in arsenic-rich environments (Bhattacharjee & Rosen, 2007). While not a traditional target for human clinical therapeutics, ArsA is a critical focus in the study of antimicrobial resistance and environmental microbiology. Understanding its structure and function offers potential for developing inhibitors to sensitize resistant bacteria or for engineering organisms for bioremediation.

Other names

Arsenite-transporting ATPaseArsenical-resistance protein ArsAArsenite-translocating ATPaseATP-dependent arsenite efflux pumpArsA ATPase

Active efflux of toxic metalloids (arsenite and antimonite) from the cytoplasm using energy derived from ATP hydrolysis.