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accessory factor UbiK family protein
BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro. [1]. 18616282. Brucella abortus MFP: a trimeric coiled-coil protein with membrane fusogenic activity. Carrica Mdel C, Craig PO, Alonso Sdel V, Goldbaum FA, Cravero SL;. Biochemistry. 2008;47:8165-8175. (from Pfam)
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