1 Parent Features
DB identifier | Type | Name |
---|---|---|
IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |
Type: | Domain | Name: | EngA-type guanine nucleotide-binding (G) domain |
Description: | The P-loop guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling,and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state andan active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G)domain that is responsible for binding and hydrolysis of guanine nucleotides.EngA (Essential neisserial GTPase A) proteins belong to TrmE-Era-EngA-YihA- Septin like superfamily of TRAFAC class and form a unique family of bacterialGTPases with two G domains in tandem, namely GD1 and GD2, followed by a C- terminal KH-like domain. They have been shown to interact with the bacterialribosome and to be involved in its biogenesis [, , , , ].The EngA-type G domains consist of ~159-170 amino acid residues and show sequence homology to the Era-type G domain. The EngA-type G domain has thusalso been termed Der, because it has double Era-like G domains []. The EngA-type G domain is composed of 5 alpha helices and 6 beta sheets linked by characteristic loops constituting switch I and II. Each EngA-type G domain contains conserved residues organised in five distinct motifs numbered G1-G5. In the G1/Walker A motifs of EngA (Gx(4)GKS) or P-loop, thetwo invariant lysine residues are known to coordinate the phosphate of nucleotide. G2 (DxxG) belongs to the loop forming switch I and interacts witha Mg(2+) ion as well as the G3/Walker B motif (DxxG). G4 has a characteristic NKxD sequence that is unique to GTPases and provides specificity to GTP. TheG5 motif (SA) is less obvious. | Short Name: | G_ENGA |
DB identifier | Type | Name |
---|---|---|
IPR027417 | Domain | P-loop containing nucleoside triphosphate hydrolase |