GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

PMID:25313396

FlgM is secreted by the flagellar export apparatus in Bacillus subtilis.

Paper focuses on FlgM secretion mechanism in B. subtilis. Identifies minimal components for FlgM secretion as FliO, FliP, FliQ, FliR, FlhA, FlhB, FliF, FliG, and FliK. FliH is NOT mentioned as a required component.

"FlgM secretion is strongly enhanced by, but does not strictly require, hook-basal body completion and instead demands a minimal subset of flagellar proteins that includes the FliF/FliG basal body proteins, the flagellar type III export apparatus components FliO, FliP, FliQ, FliR, FlhA, and FlhB, and the substrate specificity switch regulator FliK."

PMID:33572887

Protein Export via the Type III Secretion System of the Bacterial Flagellum.

Review describing FliH as part of the ATPase module (FliH-FliI-FliJ) of the flagellar type III secretion system. FliH forms FliH2-FliI1 complex and is located at the cytoplasmic face of the basal body.

"The T3SS is composed of an export gate (FliPQR/FlhA/FlhB) located in the flagellar basal body and an associated soluble ATPase complex in the cytoplasm (FliHIJ)."
The ATPase complex facilitates substrate docking and unfolding in the export process.

"The soluble ATPase complex made of FliHIJ is part of the export apparatus and thought to facilitate docking and unfolding of substrates [17]."

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.

Foundational study demonstrating that FliH binds FliI and inhibits its ATPase activity in Salmonella. Establishes FliH as a negative regulator of the ATPase.

"The ATPase activity of the FliH-FliI complex was about 10-fold lower than that of FliI alone; the presence or absence of ATP did not affect the formation of the complex."
FliH forms a homodimer that binds FliI monomer to form a FliH2-FliI complex.

"Analytical gel filtration with in-line multiangle light scattering indicated that FliH alone forms a dimer, FliI alone remains as a monomer, and FliH and FliI together form a (FliH)2FliI complex."

file:BACSU/fliH/fliH-deep-research-falcon.md

Deep research summary for B. subtilis fliH

FliH is a cytosolic component of the fT3SS export apparatus that forms a complex with FliI to regulate ATPase activity.

"Primary function: Cytosolic component of the fT3SS export apparatus that forms a complex with FliI (and FliJ) to regulate ATPase activity, dock/export chaperone-substrate complexes, and couple ATP hydrolysis to PMF-driven translocation through FlhA/FlhB/FliPQR."