Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius.
Growth of the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius strain ATCC 27009 on maltose resulted in the increased production of a protein with apparent molecular mass of 40 kDa. By metabolic labelling with 14C-palmitic acid, the 40-kDa protein was identified as a lipoprotein. The protein exhibited maltose-binding activity at pH 3.5, as demonstrated by chromatography on cross-linked amylose. Partial amino acid sequence analysis revealed that the 40-kDa protein corresponds to the product of an open reading frame downstream from the amylase gene (amy) that displays similarity to enterobacterial maltose-binding proteins.
Herrmann
A
A
Institut für Biologie, Humboldt-Universität zu Berlin, Germany.
Schlösser
A
A
Schmid
R
R
Schneider
E
E
D000595:Amino Acid Sequence; D001407:Bacillus / Q000145:classification / Q000254:growth & development / Q000502:physiology*; D002352:Carrier Proteins; D002850:Chromatography, Gel; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008074:Lipoproteins / Q000737:chemistry* / Q000378:metabolism; D008320:Maltose / Q000378:metabolism; D016366:Open Reading Frames
D002352:Carrier Proteins; D008074:Lipoproteins; D008320:Maltose