The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease.

摘要: Biochemical, immunological, and sequence analyses demonstrated that the glucose permease of Bacillus subtilis, glucose-specific Enzyme II phosphoenolpyruvate-dependent phosphotransferase system, is a single polypeptide chain with C-terminal III-like domain. A flexible hydrophilic linker, similar in length amino acid composition to linkers previously identified other regulatory or sensory transducing proteins, functions tether IIIGlc-like domain protein membrane-embedded IIGlc. Evidence presented demonstrating plays dual role transport phosphorylation both sucrose. The sucrose appears lack sucrose-specific separate, soluble IIIScr protein. IIScr was capable utilizing regardless whether IIIGlc provided as purified, protein, membrane-bound within same membrane IIScr, fragments different from those bearing IIScr. These observations suggest an autonomous structural unit assumes conformation independent hydrophobic, N-terminal intramembranal Preferential uptake over has been by vivo studies vitro assays. Addition purified strongly stimulated sucrose, but not glucose, assays contained two sugars simultaneously. results preferential determined competition corresponding sugar-specific permeases for common P approximately IIIGlc/Scr