The primary structure of Bacillus subtilis acidic ribonsomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence.
The complete primary structure of Bacillus subtilis acidic protein B-L9, functionally equivalent to protein L7/L12 from E. coli, has been determined. B-L9 is composed of 122 residues and has the amino acid composition: Asp3, ASN3, Thr4, Ser3, Glu22, Gln1, Pro3, Gly11, Ala21, Val14, Ile9, Leu12, Phe2, Lys13, and Arg1. The molecular weight of B-L9 is 12,633. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequenator, and micro dansyl-Edman degradation of the peptides obtained from digestions with trypsin, thermolysin, Staphylococcus aureus protease, chymotrypsin and pepsin. A comparison of protein B-L9 from B. subtilis with E-L12 from E. coli shows a relatively high degree of homology.
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000032:analysis*; D002918:Chymotrypsin; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D012269:Ribosomal Proteins / Q000302:isolation & purification; D013211:Staphylococcus aureus / Q000201:enzymology; D013820:Thermolysin; D014357:Trypsin
D010446:Peptide Fragments; D012269:Ribosomal Proteins; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin; D013820:Thermolysin