Li Y, Ferenci T
Department of Microbiology, University of Sydney, NSW, Australia.
Gene. 1997 Aug 22;195(2):195-200. doi: 10.1016/s0378-1119(97)00139-x.
The nucleotide sequence of the surP and surT genes in a sucrose-utilisation cluster cloned from Bacillus stearothermophilus NUB36 was determined. The surP gene encoded a protein of 466 amino acid residues and shared 60-62% amino acid identity with the sucrose-specific enzyme II components of the phosphotransferase system of Bacillus subtilis, Salmonella typhimurium and Klebsiella pneumoniae. SurP, like other sucrose EIIs, lacked the hydrophilic domain containing the first (IIA) phosphorylation site. The surT gene encoded a 278 amino acid polypeptide which showed 63.1% and 54% amino acid identity to the B. subtilis antiterminators SacT and SacY, respectively. A region containing a palindromic structure preceding surP was highly homologous to the regulatory transcription termination regions of the sacPA and sacB operons of B. subtilis and the bgl operon of Escherichia coli. Hence the sucrose gene cluster of B. stearothermophilus NUB36 is very similar to the B. subtilis sacPA operon in terms of gene order and regulatory organisation.
