A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting five functionally distinct domains: three cytoplasmic domains A, N, and P which contain the catalytic sites, and two transmembrane domains. The N domain phosphorylates the P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by the A domain. The phosphorylation and dephosphorylation cycles drive conformational changes in the protein between two states (E1 and E2), which allow the substrate to access the other side of the membrane.

Synonyms: Phosphorylation type Adenosine Triphosphatases, P-type ATPases, ATPase, P-type, ATPases, P-type, E1 E2 ATPases, P type Adenosine Triphosphatase, P type ATPase, P type Adenosine Triphosphatases, ATPases, E1-E2, Triphosphatases, Phosphorylation-type Adenosine, P-type Adenosine Triphosphatase, E1-E2 ATPases, Triphosphatases, P-type Adenosine, ATPases, Phosphorylation-type, Adenosine Triphosphatases, P-type, Triphosphatase, P-type Adenosine, P type ATPases, P-type Adenosine Triphosphatases, Adenosine Triphosphatase, P-type, Phosphorylation type ATPases, Adenosine Triphosphatases, Phosphorylation-type, EC 3.6.3.-, Phosphorylation-type Adenosine Triphosphatases, P-type ATPase, Phosphorylation-type ATPases