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Sequence of the Gene Encoding an Alkaline Serine Proteinase of Bacillus pumilus TYO‐67
Author(s) -
Aoyama Misako,
Toma Claudia,
Yasuda Masaaki,
Iwanaga Masaaki
Publication year - 2000
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2000.tb02511.x
Subject(s) - biology , subtilisin , open reading frame , serine , peptide sequence , bacillus pumilus , nucleic acid sequence , biochemistry , gene , amino acid , microbiology and biotechnology , sequence analysis , genetics , enzyme , bacteria
The complete nucleotide sequence of the gene encoding an alkaline serine proteinase ( aprP ) of Bacillus pumilus TYO‐67 was determined. The sequence analysis showed an open reading frame of 1,149 bp (383 amino acids) that encoded a signal peptide consisting of 29 residues and a propeptide of 79 residues. The deduced 3 amino acid residues, D 32 , H 64 , and S 221 , were identical with 3 essential amino acids in the catalytic center of subtilases. The sequence around these residues revealed that APRP was a new member of the true subtilisin subgroup of the subtilisin family. The highest homology was found in subtilisin NAT at 64.4% in the DNA sequence. The residue S 189 of APRP was different from those of other subtilases.