Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

Combined Automated Annotation using Multiple IEA Methods

Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits.

fliI mutants fail to regrow filaments. The sequence resembles F1-beta. This paper proposed the protein-translocase or "proton translocase" hypothesis that UniProt's FUNCTION text still reproduces.

PMID:8491729

Genetic and biochemical analysis of Salmonella typhimurium FliI, a flagellar protein related to the catalytic subunit of the F0F1 ATPase and to virulence proteins of mammalian and plant pathogens.

Catalytic-residue mutants abolish flagellation. Purified FliI binds ATP, and anti-F1-beta antibody cross-reacts with it.

PMID:8943245

Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium.

Mg2+-dependent ATPase, insensitive to F-, V- and P-type inhibitors. Walker mutants block flagellar assembly.

PMID:10998179

FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity.

FliH binds the FliI N-terminus and inhibits FliI ATPase activity.

PMID:10712687

Interactions among components of the Salmonella flagellar export apparatus and its substrates.

The FliH-FliI-FliJ soluble complex binds substrates and delivers them to the FlhA/FlhB membrane complex for ATP-dependent export.

PMID:12787361

Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly.

FliI forms ATP-promoted sixfold rings, and activity is cooperative and coupled to oligomerization.

PMID:17202259

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits.

The crystal structure of Salmonella FliI resembles F1 alpha/beta. This paralogy explains the ATP synthase labels.

PMID:18216858

Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export.

ATP hydrolysis by FliI releases the FliH-FliI escort. The PMF drives translocation, and FliH/FliI can be bypassed by FlhA/FlhB mutations.

PMID:18216859

Energy source of flagellar type III secretion.

The flagellar secretion apparatus is a proton-driven protein exporter.

PMID:20421493

Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners.

FliI binds the export chaperone FliT, and the FliT C-terminal helix regulates that binding.

PMID:21278755

Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.

FliJ resembles the gamma-subunit coiled coil and binds the centre of the FliI hexamer ring.

PMID:21934659

An energy transduction mechanism used in bacterial flagellar type III protein export.

The export gate complex is a proton-protein antiporter. FliH-FliI brings about FliJ-FlhA binding, which turns the gate into an efficient delta-psi-driven exporter.

PMID:25393010

ATPase-independent type-III protein secretion in Salmonella enterica.

Raising the PMF and substrate levels allows functional flagella to form without type III ATPase activity.

PMID:25531309

The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis.

E211D reduces ATPase activity about 100-fold, yet most cells remain motile. E211 is the catalytic base.

PMID:26916245

FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella.

FliI exists as a FliI6 ring bound in the C ring and as cytoplasmic FliH2FliI. FliH/FliI enforce FlhA interactions for energy coupling.

PMID:29946050

In Vitro Reconstitution of Functional Type III Protein Export and Insights into Flagellar Assembly.

In vitro, export needs Mg-ATP, FliJ and FliH2/FliI. ATP hydrolysis by FliI can drive export without PMF, and FlhA has ion-channel activity.

PMID:33846530

A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.

The FliI N-terminal positive-charge cluster regulates ring formation. The ring docks through FliH to FlhA and FliN.

PMID:38531947

FliH and FliI help FlhA bring strict order to flagellar protein export in Salmonella.

FliH/FliI help FlhA enforce the rod/hook to filament export order.

file:SALTY/fliI/fliI-deep-research-falcon.md

Falcon deep research report for Salmonella FliI