ATPase chaperone, AAA-type, MoxR, predicted
InterPro Protein Domain record
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description
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<p>AAA ATPases (ATPases Associated with diverse cellular Activities) form a large protein family and play a number of roles in the cell including cell-cycle regulation, protein proteolysis and disaggregation, organelle biogenesis and intracellular transport. Some of them function as molecular chaperones, subunits of proteolytic complexes or independent proteases (FtsH, Lon). They also act as DNA helicases and transcription factors [<cite idref="PUB00043605"/>].</p> <p>AAA ATPases belong to the AAA+ superfamily of ringshaped P-loop NTPases, which act via the energy-dependent unfolding of macromolecules [<cite idref="PUB00014779"/>, <cite idref="PUB00043606"/>]. There are six major clades of AAA domains (proteasome subunits, metalloproteases, domains D1 and D2 of ATPases with two AAA domains, the MSP1/katanin/spastin group and BCS1 and it homologues), as well as a number of deeply branching minor clades [<cite idref="PUB00014779"/>].</p><p>They assemble into oligomeric assemblies (often hexamers) that form a ring-shaped structure with a central pore. These proteins produce a molecular motor that couples ATP binding and hydrolysis to changes in conformational states that act upon a target substrate, either translocating or remodelling it [<cite idref="PUB00033933"/>].</p><p>They are found in all living organisms and share the common feature of the presence of a highly conserved AAA domain called the AAA module. This domain is responsible for ATP binding and hydrolysis. It contains 200-250 residues, among them there are two classical motifs, Walker A (GX4GKT) and Walker B (HyDE) [<cite idref="PUB00043605"/>].</p><p>This group represents a predicted AAA-type ATPase enzymatic complex assembly chaperone, MoxR type. The AAA+ ATPases contain a P-loop NTPase domain and function as molecular chaperones, ATPase subunits of proteases, helicases or nucleic-acid-stimulated ATPases [<cite idref="PUB00014778"/>]. AAA+ ATPases employ the energy obtained from ATP hydrolysis to remodel proteins, DNA, or RNA [<cite idref="PUB00043412"/>].</p><p>MoxR AAA+ family is a large, diverse group of ATPases that are defined by a distinct insert in helix-2 of the conserved ATPase core and an additional helical segment between the core ATPase domain and the C-terminal alpha-helical bundle [<cite idref="PUB00014778"/>]. The MoxR family can be divided into at least seven subfamilies: MoxR Proper (MRP), TM0930, RavA, CGN, APE2220, PA2707, and YehL. RavA interacts with inducible lysine decarboxylase [<cite idref="PUB00043412"/>]. MoxR AAA+ proteins generally function with VWA domain-containing proteins to form a chaperone system that is important for the folding or activation of proteins and protein complexes by mediating the insertion of metal cofactors into the substrate molecules. They are found throughout the Bacteria and Archaea, but have not yet been detected in Eukaryota [<cite idref="PUB00043413"/>].</p>
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ATPase chaperone, AAA-type, MoxR, predicted
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