Sur7　is　one　of　multiple　proteins　constituting　MCC　(membrane　compartment　of　Can1　acting　as　an　arginine/H(+)symporter),　a　crucial　membrane　domain　that　can　form　punctuate　eisosome　spots　on　the　plasma　membrane　and　execute　diverse　functions　in　model　yeast　but　remains　poorly　understood　in　filamentous　fungi.　Here,　a　Sur7　homolog　bearing　a　typical　SUR7　domain　and　four　transmembrane　domains　was　shown　to　localize　in　the　conidial　vesicles　and　enter　vacuoles　and　appear　sporadically　on　the　periphery　membrane　during　hyphal　growth　in　the　insect-pathogenic　fungusBeauveria　bassiana,　implicating　an　involvement　of　Sur7　in　cellular　events　linked　to　both　plasma　membrane　and　vacuoles.　Deletion　ofsur7resulted　in　reduced　conidiation　capacity　and　impaired　conidial　quality,　which　was　featured　by　slower　germination,　attenuated　virulence,　and　reduced　carbohydrate　epitopes　(beta-N-acetylglucosamine　and　sialic　acids).　Also,　the　hyphal　cell　walls　of　the　deletion　mutant　were　severely　impaired　due　to　similar　to　70%　reductions　in　chitin　and　neutral　carbohydrate　contents　and　a　moderate　increase　in　alkali-soluble　carbohydrate　content.　Consequently,　the　deletion　mutant　became　more　sensitive　to　three　cell　wall　perturbing　chemicals　(Congo　red,　calcofluor　white,　and　SDS)　and　an　antifungal　drug　(caspofungin)　and　surprisingly　showed　a　hypersensitivity　to　oxidative　stress　of　H(2)O(2)and　an　increased　sensitivity　to　osmotic　stress　of　NaCl　or　sorbitol.　Its　hypersensitivity　to　H(2)O(2)was　associated　with　transcriptional　repression　of　critical　catalase　genes　required　for　H(2)O(2)decomposition.　These　findings　unveil　that　Sur7　takes　part　in　both　MCC/eisosome　and　vacuolar　events　and　hence　acts　as　a　sustainer　of　conidiation　capacity,　cell　wall　integrity,　multiple　stress　tolerance,　and　virulence　inB.　bassiana.