Homologous Superfamily

P-loop containing nucleoside triphosphate hydrolase (IPR027417)

Short name: P-loop_NTPase

Overlapping entries



The P-loop NTPase fold is the most prevalent domain of the several distinct nucleotide-binding protein folds.

The most common reaction catalysed by enzymes of the P-loop NTPase fold is the hydrolysis of the beta-gamma phosphate bond of a bound nucleoside triphosphate (NTP). The energy from NTP hydrolysis is typically utilised to induce conformational changes in other molecules, which constitutes the basis of the biological functions of most P-loop NTPases. P-loop NTPases show substantial substrate preference for either ATP or GTP [PMID: 15381417].

P-loop NTPases are characterised by two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motifs which bind, respectively, the beta and gamma phosphate moieties of the bound NTP, and a Mg2+ cation [PMID: 6329717].

P-loop ATPase domains belong to one of the two major divisions. The kinase-GTPase (KG) division includes the kinases and GTPases, and the ASCE division, characterised by an additional strand in the core sheet, which is located between the P-loop strand and the Walker B strand. Most members of the ASCE division utilise ATP and members of this group include AAA+, ABC, PilT, HerA-FtsK, superfamily 1/2 (SF1/2) helicases, and the RecA/ATP-synthase superfamilies of ATPases, etc [PMID: 11916378, PMID: 14568537].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.