A Tripartite Efflux System Affects Flagellum Stability in .

uses a cluster of polar, sheathed flagella for swimming motility. A search for homologs of proteins that were conserved in species that possess flagellar sheaths but were underrepresented in species with unsheathed flagella identified several candidate proteins. Four of the identified proteins are predicted to form part of a tripartite efflux system that includes two transmembrane domains of an ABC transporter (HP1487 and HP1486), a periplasmic membrane fusion protein (HP1488), and a TolC-like outer membrane efflux protein (HP1489).

Loss of a Cardiolipin Synthase in G27 Blocks Flagellum Assembly.

uses a cluster of polar, sheathed flagella for motility, which it requires for colonization of the gastric epithelium in humans. As part of a study to identify factors that contribute to localization of the flagella to the cell pole, we disrupted a gene encoding a cardiolipin synthase () in strains G27 and B128. Flagellum biosynthesis was abolished in the G27 mutant but not in the B128 mutant.