D-secretion capability in EMV fractions than Escherichia coli, and its EMVs include a significant protein (P49), which can be not necessary for vesicle production. We applied mutant EMVs that lack P49 to recognize minor components of EMVs that may control vesiculation. Methods: EMVs had been subjected to 2D gel-based proteomics by peptide mass fingerprinting. Inside the identified proteins, the function of a sensor protein homolog, HM1275, was analysed by swarming assay and lipid-staining to quantify EMVs made in different media. Changes in the quantity of EMVsJOURNAL OF EXTRACELLULAR VESICLESdepending on culture media were quantified by tunable resistive pulse sensing method. Outcomes: A protein with a PAS domain in addition to a methylaccepting chemotaxis protein (MCP) sensing domain, HM1275, was identified in the EMVs. Despite the fact that some MCPs are associated with flagellar motility by binding some attractants, the flagellar motility of Delta-hm1275 was not significantly distinct from that of WT. Despite the fact that the amounts of EMVs produced by WT had been increased in response towards the PRMT5 Species concentration of casamino acids in poor nutrient medium, these by Delta-hm1275 were not. Summary/conclusion: A putative sensor protein, HM1275, was identified in EMVs and may perhaps recognize the extracellular environments by binding signal molecules in casamino acids to control vesiculation. Although further studies are necessary to reveal the signals and also the sensing pathways, the results obtained within this study indicate that bacterial vesiculation is controlled by extracellular environments, and artificial manage of vesiculation with extracellular signals will be useful in applications like suppression of vesicle-dependent pathogenicity. Funding: Japan Society for Promotion of Science Study Fellowship for Young ScientistsPT05.05=OWP2.Prokaryotic BAR domain-like protein BdpA promotes outer membrane extensions Daniel A. Phillipsa, Lori Zacharoffb, Cheri Hamptonc, Grace Chongb, Brian Eddied, Anthony Malanoskid, Shuai Xub, Lauren Ann Metskase, Lina Birdf, Grant Jensene, Lawrence Drummyc, Moh El-Naggarb and Sarah Glavenda American Society for Engineering Education U.S. Naval Study Laboratory, Washington, USA; bUniversity of Southern California, Los Angeles, USA; cMaterials and Manufacturing Directorate, Air Force Analysis Laboratory, Dayton, USA; dU.S. Naval Research Laboratory, Washington, USA; eCalifornia Institute of Technology, Pasadena, USA; f National Analysis Council, Washington, USAIntroduction: Bin/Amphiphysin/RVS (BAR) STAT3 Storage & Stability domains belong to a superfamily of membrane-associated coiled-coil proteins that influence membrane curvature. BAR domains are ubiquitous in eukaryotes and connected with membrane curvature formation, vesicle biogenesis/trafficking, protein scaffolding andintracellular signalling. Whilst advances in protein domain prediction have facilitated the identification of numerous BAR domain proteins, they’ve but to become characterized in bacteria. Here, we identified a putative BAR domain-containing protein enriched in the outer membrane vesicles (OMVs) of Shewanella oneidensis MR-1, a dissimilatory metal-reducing bacteria known to produce outer membrane extensions (OMEs) which are suspected to facilitate extended distance extracellular electron transfer (EET) but whose physiological relevance and mechanism of formation remain unknown. Techniques: Purified S. oneidensis OMVs had been prepared by filtration and ultracentrifugation for comparative proteomics with cell-associated outer membrane proteins or.