fliF

Summary: FliF contributes to the proton-driven flagellar motor through the assembled rotor.

Reason: Current GO:0003774 explicitly includes flagellar rotation powered by an electrochemical proton gradient, and GO:0140605 is its is_a descendant. The replacement is therefore a genuine refinement to proton-motive-force-driven motor activity. FliF contributes the assembled MS-ring rotor structure; this does not assert autonomous proton translocation or torque generation by isolated FliF. The comparative structural evidence is transferred to the KT2440 homolog, not a target-specific motor assay.

Proposed replacements: proton motive force-driven motor activity

Summary: The FliF MS ring is embedded in the cytoplasmic membrane.

Reason: Correct membrane localization.

Summary: FliF occupies the bacterial-type flagellum basal body, MS ring.

Reason: The broader location is sound but the conserved component architecture supports this specific flagellar substructure. This is a target-family inference from comparative structures, not a KT2440 localization experiment.

Proposed replacements: bacterial-type flagellum basal body, MS ring

Summary: FliF oligomers form the MS ring.

Reason: This is the most specific and informative component annotation.

Summary: FliF is a structural part of the rotating flagellar apparatus.

Reason: The subunit contributes the physical rotor or torque-transmitting rod used during motility. This is direct structural participation, inferred from conserved architecture; exact target kinetics and surface behaviors are not inferred.

Summary: FliF oligomerizes to form the structural MS ring of the flagellar basal body.

Reason: Structural molecule activity captures the direct molecular role of this ring-forming subunit. Membership is from family classification: Q88ET4 matches the NCBIfam TIGR00206 FliF model and the curated PIRNR FliF family assignment. The structural role is ortholog evidence from Salmonella, where the MS ring is a complex made of FliF that is the base of flagellar structure (PMID:34244518); it has not been tested for KT2440 FliF.

Summary: FliF forms the MS ring during bacterial flagellum assembly.

Reason: The structural role is a direct required step in basal-body assembly: FliF subunits themselves assemble into the MS ring, and in Salmonella conserved FliF residues are needed for MS-ring formation and for assembly of the export apparatus and rod within it (PMID:34244518). This is ortholog evidence transferred by family membership (NCBIfam TIGR00206 fliF), not a KT2440 experiment.