flagellated

Edge evidence

• flagellar filament enables flagellated RO:0002327

  A flagellar filament is the locomotory appendage of flagellated cells.

  • DOI:10.3390/biom9070279 helical filamentous organelle responsible for motility Supports the filament as the locomotory flagellar structure.
• flagellar hook connects flagellar filament

  The hook couples the motor to the filament.

  • DOI:10.3390/biom9070279 hook as a universal joint Supports the hook's coupling role.
• flagellar basal body rotates flagellar filament

  The basal body motor rotates the filament for propulsion.

  • DOI:10.1016/S1937-6448(08)01402-0 reversible rotary motor Supports basal body motor rotation of flagella.
• ion motive force enables flagellar stator complex RO:0002327

  Ion flux through stator complexes powers torque generation.

  • DOI:10.3389/fmicb.2021.659464 relationship between the IMF and the functioning Supports ion motive force coupling to flagellar motor function.
• chemotaxis signaling regulates flagellated RO:0002211

  Chemotaxis signaling changes flagellar motor behavior and movement direction.

  • DOI:10.3390/biom9070279 regulate the direction of flagella-driven motility Supports chemotaxis regulation of flagellated motility.
• flagellar type III secretion system exports flagellar structural subunits METPO:2000209

  The fT3SS exports flagellar structural subunits to the distal assembly site.

  • DOI:10.1128/ecosalplus.esp-0011-2023 "a flagellar type III secretion system (fT3SS) at the base exports structural subunits from the cytoplasm through a narrow central channel to the distal tip where assembly occurs"
• FliH-FliI-FliJ ATPase complex enables flagellar type III secretion system RO:0002327

  The FliH-FliI-FliJ ATPase complex powers flagellar protein export by the fT3SS.

  • DOI:10.1128/ecosalplus.esp-0011-2023 "the ATPase ring complex (FliI, with FliH and FliJ) provides ATP hydrolysis for export"
• FliD filament cap enables flagellar filament polymerization RO:0002327

  The FliD filament cap aids polymerization of flagellin into the filament.

  • DOI:10.3390/biom14121488 "flagellin subunits (~30,000) polymerize into a filament aided by a five-subunit FliD cap"
• FlgK/FlgL hook-filament junction enables flagellar filament polymerization RO:0002327

  FlgK/FlgL hook-filament junction proteins are required for filament polymerization.

  • DOI:10.3390/biom14121488 "absence of FlgK/FlgL/FliD prevents filament polymerization"
• flagellar filament polymerization results in formation of flagellar filament

  Polymerization of flagellin subunits forms the flagellar filament.

  • DOI:10.3390/biom14121488 "flagellin subunits (~30,000) polymerize into a filament" forming the helical filament.
• flagellar stator complex has function transmembrane H+ channel RO:0000085

  The MotA-MotB stator complex acts as a transmembrane H+ channel powering rotation.

  • DOI:10.3390/biom14121488 "stator units formed by MotA and MotB ... act as a transmembrane H+ channel"
• CheY-P regulates flagellar rotational switching RO:0002211

  CheY-P binding to the C ring causes flagellar rotational switching (CCW/CW).

  • DOI:10.1038/s41564-024-01630-z "Directional switching is triggered by the chemotaxis regulator CheY-P binding to FliM, causing full reversal of rotation"
• flagellar rotational switching regulates flagellated RO:0002211

  Switching of motor rotation direction modulates flagellated motility behavior.

  • DOI:10.1128/ecosalplus.esp-0011-2023 "the C ring switches its conformational state" changing the direction of flagella-driven motility.