Polar landmark protein HubP recruits flagella assembly protein FapA under glucose limitation in Vibrio vulnificus

Summary How motile bacteria recognize their environment and decide whether to stay or navigate toward more favorable location is a fundamental issue in survival. The flagellum is an elaborate molecular device responsible for bacterial locomotion, and the flagellum‐driven motility allows bacteria to move themselves to the appropriate location at the right time. Here, we identify the polar landmark protein HubP as a modulator of polar flagellation that recruits the flagellar assembly protein FapA to the old cell pole, thereby controlling its activity for the early events of flagellar assembly in Vibrio vulnificus. We show that dephosphorylated EIIAGlc of the PEP‐dependent sugar transporting phosphotransferase system sequesters FapA from HubP in response to glucose and hence inhibits FapA‐mediated flagellation. Thus, flagellar assembly and motility is governed by spatiotemporal control of FapA, which is orchestrated by the competition between dephosphorylated EIIAGlc and HubP, in the human pathogen V. vulnificus. How motile bacteria recognize their environment and decide whether to stay or move is a fundamental issue in survival. Here we established the molecular mechanism underlying the intimate relationship between nutrient availability and flagellum‐driven motility in Vibrio vulnificus; dephosphorylated EIIAGlc of the PEP:carbohydrate phosphotransferase system sequesters the flagellar assembly protein FapA from the polar landmark protein HubP in response to glucose, and hence inhibits the FapA‐mediated flagellation. Thus, spatiotemporal regulation of FapA facilitates flagellation and motility.