ATPase

ATPase is an enzyme which catalyzes the breakdown of ATP into ADP and a phosphate ion. This dephosphorylation releases energy which the enzyme uses to drive other reactions^[1]. The F1/0 ATPase is called ATP synthase synthesises the reverse reaction, i.e., the addition of phosphate to ADP to form ATP^[2]. ATPase types include:

• F-ATPase - the prime producers of ATP. For details see Alice Clark/ATPsynthase;
  
• V-ATPase or Vacuolar-type H+ ATPase couples the energy to proton transport across membranes. For details see V-ATPase;
  
• A-ATPase are found in archaea. For details see A-ATP Synthase;
  
• P-ATPase transport ions;
  
• E-ATPase hydrolyze extracellular ATP.
  
• MipZ is an ATPase which forms a complex with the chromosome partitioning protein ParB and is responsible for the regulation of FtsZ ring formation.
  

ATPase domains include metal-binding domain (MBD) and nucleotide-binding domain (NBD). For more details see:

• Cu transporting ATPase are in P(1B)-Type Cu(I) Transporting ATPases ATP7A and ATP7B.
  
• Na/K transporting ATPase are in Sodium-Potassium ATPase.
  
• H/K transporting ATPase are in Esomeprazole and H+/K+ - ATPase Interaction.
  
• Transitional endoplasmic reticulum ATPase are in Valosin Containing Protein D120.
  
• Central stalk in F(1)-ATPase is described in A-ATP Synthase
  
• RuvBL1/RuvBL2 complex (ATPase)
  
• For Ter-ATPase see Valosin Containing Protein D120