The AAA+ superfamily of ATPases is found in all kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Although the terms AAA+ and AAA are often used loosely and interchangeably, the classical AAA family members are distinguished by their possession of the SRH region in the AAA module. Many AAA+ proteins are involved in similar processes to those of AAA proteins (facilitation of protein folding and unfolding, assembly or disassembly of proteins complexes, protein transport and degradation), but others function in replication, recombination, repair and transcription. For a review see [1].

The proteins in this superfamily are characterised by the structural conservation of a central ATPase domain of about 250 amino acids called the AAA+ module. Typically, the AAA+ domain can be divided into two structural subdomains, an N-terminal P-loop NTPase alpha-beta-alpha subdomain that is connected to a smaller C-terminal all-alpha subdomain. The alpha-beta-alpha subdomain adopts a Rossman fold and contains several motifs involved in ATP binding and hydrolysis, including classical motifs Walker A and Walker B [2, 2]. The all-alpha subdomain [3], is much less conserved across AAA+ proteins.

1. AAA+ superfamily ATPases: common structure--diverse function. Genes Cells 6, 575-97
2. The AAA+ superfamily of functionally diverse proteins. Genome Biol. 9, 216
3. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43

The AAA+ superfamily of ATPases is found in all kingdoms of living organisms where they participa
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