InterPro domain: IPR022878

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [ 1 , 2 ]. The different types include:

• F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
• V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [ 3 ]. They are also found in bacteria [ 4 ].
• A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [ 5 , 6 ].
• P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
• E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

This entry represents the catalytic subunit alpha of V-type ATP synthase, which is known as subunit A in eukaryotes. In bacteria and archaea it produces ATP from ADP in the presence of a proton gradient across the membrane.

1. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett. 576, 1-4
2. Mechanisms of ATPases--a multi-disciplinary approach. Curr. Protein Pept. Sci. 5, 89-105
3. Regulation and isoform function of the V-ATPases. Biochemistry 49, 4715-23
4. F-and V-ATPases in the genus Thermus and related species. Syst. Appl. Microbiol. 21, 12-22
5. New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). Bioessays 30, 1096-109
6. F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. Biochim. Biophys. Acta 1101, 232-5