P-type ATPases

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.

Also Known As:

E1-E2 ATPases; P-type Adenosine Triphosphatases; Phosphorylation-type ATPases; Phosphorylation-type Adenosine Triphosphatases; ATPase, E1-E2; ATPase, P-type; ATPases, E1-E2; ATPases, P-type; ATPases, Phosphorylation-type; Adenosine Triphosphatase, P-type; Adenosine Triphosphatases, P-type; Adenosine Triphosphatases, Phosphorylation-type; Atpase, P Type; E1 E2 ATPase; E1 E2 ATPases; P type ATPases; P type Adenosine Triphosphatase; P type Adenosine Triphosphatases; Phosphorylation type ATPases; Phosphorylation type Adenosine Triphosphatases; Triphosphatase, P-type Adenosine; Triphosphatases, P-type Adenosine; Triphosphatases, Phosphorylation-type Adenosine; Type Atpase, P; E1-E2 ATPase; P Type Atpase; P-type ATPase; P-type Adenosine Triphosphatase

Enzymes and Coenzymes: 1
- Enzymes: 152586
  - Hydrolases: 2166
    - Acid Anhydride Hydrolases
      - Adenosine Triphosphatases: 8623
        P-type ATPases: 226
Amino Acids, Peptides, and Proteins: 1
- Proteins: 484843
  - Carrier Proteins: 12999
    - Membrane Transport Proteins: 589
      - P-type ATPases: 226
  - Membrane Proteins: 10078
    - Membrane Transport Proteins: 589
      - P-type ATPases: 226

Arabidopsis ECA4 protein

Bio-Agent Context: Research Results