Location of enzymatic and DNA-binding domains on E. coli protease La.
Escherichia coli protease La is an ATP-dependent enzyme that has a DNA-binding site. The locations of the enzymatic and DNA-binding sites are not known. We report that a 75-residue segment at the carboxy-terminus of the protease La is similar to part of Bacillus licheniformis beta-lactamase, a serine enzyme. The comparison score is 8.2 standard deviations higher than that obtained with 10,000 comparisons of randomized sequences of these segments. The probability of obtaining such a score by chance is 1.2 x 10(-16). We also find that a 107-residue segment in the amino-terminus half of protease La is similar to part of the sopB protein, a DNA-binding protein of the plasmid F of E. coli. The comparison score for these segments is 8 standard deviations (P = 6 x 10(-16)). These strong amino acid sequence similarities suggest the locations of the catalytic serine and the DNA-binding domains of protease La.
Baker
M E
ME
Department of Medicine, University of California, San Diego, La Jolla 92093.
D049069:ATP-Dependent Proteases; D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins; D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000378:metabolism*; D001618:beta-Lactamases
D004268:DNA-Binding Proteins; D006360:Heat-Shock Proteins; D004247:DNA; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D001618:beta-Lactamases