EC Number   |
General Information |
Reference |
|---|
   7.4.2.8 | evolution |
ATPase DotB belongs to the VirB11 family of proteins, but sequence analysis reveals that DotB might be more related to PilT/EpsE family proteins than VirB11 family proteins. The subunits DotBL from Legionella pneumophila and DotBY from Yersinia pseudotuberculosis display a very similar topology |
-, 752136 |
| 7.4.2.8 | evolution |
ATPase DotB belongs to the VirB11 family of proteins, but sequence analysis reveals that DotB might be more related to PilT/EpsE family proteins than VirB11 family proteins. The subunits DotBL from Legionella pneumophila and DotBY from Yersinia pseudotuberculosis display a very similar topology. The N-terminal domain of DotBL adopts a PAS-like fold, similar to PilT, EpsE, and HP0525 |
752136 |
| 7.4.2.8 | evolution |
enzyme FliI is a member of the Walker-type ATPase family |
733409 |
| 7.4.2.8 | evolution |
EpsE is a AAA+ ATPase and member of the bacterial Type II/IV secretion subfamily of NTPases |
-, 757525 |
| 7.4.2.8 | evolution |
phylogenetic analysis and tree of T3SS ATPases, overview |
734010 |
| 7.4.2.8 | evolution |
the enzyme contains a two-helix-finger motif at the entrance of the modeled central pore of the InvC hexamer. The motif is highly conserved among type III secretion-associated ATPases, including those associated with the flagellar assembly apparatus. In addition to the tyrosine residue (Tyr385 in InvC) located at the center of the loop, other residues within the loop are highly conserved, such as Gly383, Glu384, and Gly388. Similarities between type III secretion ATPases and other ATP-driven protein translocases/unfoldases |
-, 734097 |
| 7.4.2.8 | evolution |
the T2SS secretion ATPase GspE belongs to the family of Type II/IV secretion ATPases |
735288 |
| 7.4.2.8 | evolution |
VirB11 belongs to the superfamily of traffic ATPases, which includes members of the type II secretion system and the type IV pilus and archaeal flagellar assembly apparatus |
-, 734086 |
| 7.4.2.8 | malfunction |
abrogation of the interaction between the CesABEspA complex and EscN resulted in severe secretion and infection defects |
733630 |
| 7.4.2.8 | malfunction |
complementing a spa47 null Shigella flexneri strain with the inactive Spa47K165A mutant results in the same lack of invasiveness seen for the null strain. The hemolysis results presented suggest that Shigella strains lacking the gene for Spa47 or strains complemented with ATPase inactive Spa47 mutants are not able to properly insert the translocon into the host membrane. This seems to be a direct result of an inability of the mutant strains to secrete IpaB and IpaC and properly deliver them to the host cell membrane. Phenotype, overview |
751074 |
