Gene Ontology annotation through association of InterPro records with GO terms
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
A flagellar-specific ATPase (FliI) is necessary for flagellar export in Helicobacter pylori.
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H. pylori fliI mutant is non-motile and >99% aflagellate with reduced flagellin and hook protein.
"An isogenic mutant of fliI was non-motile and synthesised reduced amounts of flagellin and hook protein subunits."
Molecular characterization of a flagellar export locus of Helicobacter pylori.
Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori.
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The FliI N-terminal residues 1-18 mediate FliH binding; residues 21-91 resemble the F1-ATPase N-terminal oligomerization domain.
"residues 21-91 of FliI resemble the N-terminal oligomerization domain of the F1-ATPase catalytic subunits"
Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone.
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H. pylori FlgN chaperone binds full-length FliI and FliI(2-92) with sub-micromolar affinity.
"Hence the data indicate that FlgN, like FliT, interacts strongly with the flagellum ATPase FliI."
Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium.
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Salmonella FliI (homolog) is a Mg2+-dependent ATPase insensitive to F-type ATPase inhibitors.
"The activity was not affected by inhibitors of the F-, V- or P-type ATPases"
Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits.
ATP-induced FliI hexamerization facilitates bacterial flagellar protein export.
Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.
Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export.
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Flagellar export is PMF-driven; FliI ATP hydrolysis releases FliH-FliI from the substrate at the gate.
"The rest of the successive unfolding/translocation process of the substrates is driven by proton motive force."
Energy source of flagellar type III secretion.
An energy transduction mechanism used in bacterial flagellar type III protein export.
Falcon deep research report for H. pylori J99 fliI