Cloning and sequence of an alkaline serine protease-encoding gene from the marine bacterium Alteromonas sp. strain O-7.
The gene (aprII) encoding alkaline serine protease (AprII; subtilase) from Alteromonas sp. strain O-7 was cloned in plasmid pUC19 and transformed into Escherichia coli JM109. The nucleotide (nt) sequence of aprII has been determined. A single open reading frame (ORF) encoded a protein consisting of 621 amino acids (aa) with a M(r) of 63,958. The results of aa sequence analysis indicated that AprII is produced as a large precursor consisting of four domains: the signal sequence, the N-terminal pro-region (AprII-N), the mature AprII (AprII-M) and the C-terminal pro-region (AprII-C). The aa sequence of AprII-M shows high sequence homology with those of class-II subtilases. Two conserved sequences were found in AprII-N which might play a critical role in the maintenance of chaperone-like activity. Repeated aa sequences were observed in AprII-C (AprII-C1 and AprII-C2). The aa sequences of AprII-C1 and AprII-C2 show high sequence homology with those of the C-terminal pro-region of the other known proteases.
Tsujibo
H
H
Osaka University of Pharmaceutical Sciences, Japan.
Miyamoto
K
K
Tanaka
K
K
Kawai
M
M
Tainaka
K
K
Imada
C
C
Okami
Y
Y
Inamori
Y
Y
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D005798:Genes, Bacterial; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D012697:Serine Endopeptidases; C085501:aprII protein, Alteromonas; C032923:microbial serine proteinases