Intracellular proteinase of Bacillus subtilis.
An intracellular serine proteinase was isolated from Bacillus subtilis, strain A-50. The molecular weight of the enzyme is 30000 +/- 1000, its amino acid composition is enriched in glutamic acid residues, the isoelectric point is 4.3, the N-terminal sequence Glu-Leu-Pro-Glu-Gly-Ile-Gln-Val-Ile-Lys-Ala-Pro-Glu-Leu-Xxx-Ala-Gln-Gly-Phe-Lys Gly-Ser-Asx-Ile-Lys-Ile-Ala-Val-Leu-Asx. The enzyme is structuraly homologous with secretory subtilisins.
D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000201:enzymology*; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D012694:Serine; D013381:Subtilisins
D000596:Amino Acids; D012694:Serine; D010450:Endopeptidases; D013381:Subtilisins