Cloning and Sequence Analysis of a Protease - encoding Gene from the Marine Bacterium

The gene (trprl) encoding alkaline serine protease (Aprl; subtilase) from Atteremonas sp. strain O-7 was cloned and sequenced. The nucleotide sequence of tu7rl has been identified. The deduced arnino acid sequence indicated that uprl codes for a precursor of 715 amino acids and the precursor is composed of four regions including a signal peptide, an N-terminal pro-region, a mature protease region and a C-terminal extensioil region of 215 amino acids as preyiously described for aprll [H. Tsujibo et al., Gbne, 136, 247-251 (1993)]. The amino acid sequence of the mature Aprl (Aprl-M) showed high sequence homology with those of other class I subtilases. The C-terminat region was characterized by a repeat of 94 amino acids residues, which showed about 50'Xi similarity with those of the C-terminal pro-region of several known proteases from Gram-negatiye bacteria.