The primary structure of the DNA‐binding protein II from Clostridium pasteurianum

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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 M rof 10133. 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.