title: The primary structure of the DNA-binding protein II from Clostridium pasteurianum.
abstract: The complete amino acid sequence of the Clostridium pasteurianum DNA-binding protein II (DNAb-II) has been determined. The molecule contains 91 amino acid residues and has an Mr of 10 133. Sequence data were obtained from manual Edman degradation, using the DABITC/PITC double-coupling of the tryptic, peptic, chymotryptic and Staphylococcus protease peptides. A comparison of the amino acid sequence of the C. pasteurianum DNAb-II with those of the DNAb-II from Escherichia coli, Bacillus stearothermophilus, Thermoplasma acidophilum and Pseudomonas aeruginosa shows that the C. pasteurianum protein is more homologous to that of B. stearothermophilus (60%) than to that of E. coli (45%). All DNAb-II proteins have identical sequences Gly-Phe-Gly-X-Phe at positions 46-50 and Arg-Asn-Pro-X-Thr at positions 61-65.
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins; D003013:Clostridium / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D010446:Peptide Fragments