The complete nucleotide sequence of the gene encoding an alkaline serine pr
oteinase (aprP) of Bacillus pumilus TYO-67 was determined, The sequence ana
lysis showed an open reading frame of 1,149 bp (383 amino acids) that encod
ed a signal peptide consisting of 29 residues and a propeptide of 79 residu
es, The deduced 3 amino acid residues, D-32, H-64, and S-221, were identica
l with 3 essential amino acids in the catalytic center of subtilases. The s
equence around these residues revealed that APRP was a new member of the tr
ue subtilisin subgroup of the subtilisin family, The highest homology was f
ound in subtilisin NAT at 64.4% in the DNA sequence. The residue S-189 of A
PRP was different from those of other subtilases.