ATPase, alpha/beta subunit, nucleotide-binding domain, active site

Definition

This entry represents a 10 amino acid region that is essential for catalysis. The signature pattern contains two highly conserved serines. The first serine seems to be important for catalysis - in the ATPase alpha-chain at least - as its mutagenesis causes catalytic impairment. 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. This group of proteins include the alpha and beta subunits found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively (sometimes called the A and B subunits in V- and A-ATPases), as well as Type 3 secretion system ATPase and Flagellum-specific ATP synthase.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• ATP5F1A
• ATP5F1B
• ATP6V1A
• ATP6V1B1
• ATP6V1B2