| Description | 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 [ ]. The RsgA-type GTPase domain is predominantly bacterial, with a probable acquisition by plants from chloroplasts []. | Name | RsgA GTPase domain |
| Short Name | RsgA_GTPase_dom | Type | Domain |
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