The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase

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Abstract
The first Zn(II)-translocating P-type ATPase has been identified as the product of o732 , a potential gene identified in the sequencing of the Escherichia coli genome. This gene, termed zntA , was disrupted by insertion of a kanamycin gene through homologous recombination. The mutant strain exhibited hypersensitivity to zinc and cadmium salts but not salts of other metals, suggesting a role in zinc homeostasis in E. coli . Everted membrane vesicles from a wild-type strain accumulated 65 Zn(II) and 109 Cd(II) by using ATP as an energy source. Transport was sensitive to vanadate, an inhibitor of P-type ATPases. Membrane vesicles from the zntA ∷ kan strain did not accumulate those metal ions. Both the sensitive phenotype and transport defect of the mutant were complemented by expression of zntA on a plasmid.