• Journal of Microbiology
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• v.34 no.1
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• pp.68-73
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• 1996

An nprX gene of Bacillus subtilis NS15-4 encoding a neutral protease was cloned and its molecular characteristics were analyzed. The complete nucleotide sequence indicated that there is an open reading frame (0RF) possibly encoding 521 amino acid polypeptide. The ORF used all codons expected two cysteine and a proline having a codon bias index (CBI) of 0.09 in Escherichia coli. There were homologous sequences to the consensus sequence of -35 and -10 regions of E. coli promoters and to a Shine-Dalgarno (SD) sequence located 25 bp downstream of a mojor transcription initiation site. Moreover, there were also five minor transcription initiation sites at 6. 7. 8. 14 and 15 nt downstream of the major site. Northern blot analysis revealed the presence of about 1.8 kb mRNA transcript in E. coli having the nprX gene. The nucleotide sequence was identified in GenBank to be a gene for a neutral protease of B. sutilis with six nucleotide difference in the ORF region. The flanking regions of the NprX ORF showed much more differences form those of other neutral protease genes except the nprE gene of B. subtilis, which has the most homology to the nprX gene, and of which the flanking regions were identical to those of the nprX gene.

• Microbiology and Biotechnology Letters
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• v.18 no.3
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• pp.309-316
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• 1990

The sequence of a 1795 bp restriction fragment containing the B. circulans F-2 gene for NaC1- dependent $\alpha$-amylase (CI-amylase) is reported. The probable coding region of the gene is 1005 base pairs (335 amino acida) long. The NaC1-dependent $\alpha$-amylase (el-amy) sequence shows an open reading frame (ORF) with the translated molecular weight of about 38, 006, which correspond to a molecular weight of about 35, 000 (Mi). The gene is preceded by the sequence resembling promoter for the vegetative B, subtitis RNA polymerases. These are followed by the sequences resembling a B. subtilis ribosome binding site 5 nucleotides before the first codon of the gene. Homologous regions with other amylases were found. The N-terminal sequences of the mature proteins expressed in E. eoli were identical to the N-terminal sequences which are anaIysed.