Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661). ATP + H2O + Pb(2+)(in) = ADP + H(+) + Pb(2+)(out) + phosphate ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out) ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate Inhibited by orthovanadate. Induced by zinc. Has two high-affinity metal-binding sites, one in the N-terminal region and another in the transmembrane region. Both sites are able to access and bind metal ion independently of each other. The N-terminal metal-binding site is not strictly necessary for activity and metal selectivity, but is needed for maximal activity and may be involved in regulation. The metal-binding site in the transmembrane region is essential for activity of the pump. Mutant exhibits hypersensitivity to zinc, cadmium, lead and, to a lesser extent, cobalt and nickel. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.