InterPro domain: IPR010914

GTPases function as crucial molecular switches in a broad variety of biochemical processes. The majority of GTPases form a vast class of evolutionarily related proteins within the broader class of P-loop-containing ATPases. The P-loop GTPases share a conserved amino acid sequence G1-G3-G4 motif pattern (G2 is less well conserved) present in the GTPase domain. The Escherichia coli protein EngC (also known as RsgA) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern [ 1 ]. The RsgA-type GTPase domain is predominantly bacterial, with a probable acquisition by plants from chloroplasts [ 2 ].

1. YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. Biochemistry 41, 11109-17
2. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317, 41-72