<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Arroyo-Perez EE</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>RP93004</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11620751</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13</volume><pubmed_abstract>The coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell pole landmark protein HubP remain unclear. In this study, we discovered a novel protein called FipA that is required for normal FlhF activity and function in polar flagellar synthesis. We demonstrated that membrane-localized FipA interacts with FlhF and is required for normal flagellar synthesis in &lt;i>Vibrio parahaemolyticus&lt;/i>, &lt;i>Pseudomonas putida&lt;/i>, and &lt;i>Shewanella putrefaciens&lt;/i>, and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localizati</pubmed_abstract><journal>eLife</journal><pubmed_title>A conserved cell-pole determinant organizes proper polar flagellum formation.</pubmed_title><pmcid>PMC11620751</pmcid><funding_grant_id>TRR 174-P12</funding_grant_id><pubmed_authors>Hook JC</pubmed_authors><pubmed_authors>Arroyo-Perez EE</pubmed_authors><pubmed_authors>Wimmi S</pubmed_authors><pubmed_authors>Glatter T</pubmed_authors><pubmed_authors>Ringgaard S</pubmed_authors><pubmed_authors>Alvarado A</pubmed_authors><pubmed_authors>Thormann K</pubmed_authors></additional><is_claimable>false</is_claimable><name>A conserved cell-pole determinant organizes proper polar flagellum formation.</name><description>The coordination of cell cycle progression and flagellar synthesis is a complex process in motile bacteria. In γ-proteobacteria, the localization of the flagellum to the cell pole is mediated by the SRP-type GTPase FlhF. However, the mechanism of action of FlhF, and its relationship with the cell pole landmark protein HubP remain unclear. In this study, we discovered a novel protein called FipA that is required for normal FlhF activity and function in polar flagellar synthesis. We demonstrated that membrane-localized FipA interacts with FlhF and is required for normal flagellar synthesis in &lt;i>Vibrio parahaemolyticus&lt;/i>, &lt;i>Pseudomonas putida&lt;/i>, and &lt;i>Shewanella putrefaciens&lt;/i>, and it does so independently of the polar localization mediated by HubP. FipA exhibits a dynamic localizati</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Dec</publication><modification>2026-06-02T10:48:44.777Z</modification><creation>2025-04-03T23:52:00.641Z</creation></dates><accession>S-EPMC11620751</accession><cross_references><pubmed>39636223</pubmed><doi>10.7554/eLife.93004</doi></cross_references></HashMap>