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Bacillus  spp. are the main sources of subtilisin E, which has several applications in biotechnology. The 3D structure of subtilisin E has a significant impact on its efficacy. In this study, we evaluated subtilisin E from  Bacillus subtilis  subsp.  subtilis  str. 168 by bioinformatic methods. The results revealed that the subtilisin E sequence from  B. subtilis  contains highly conserved amino acids, including histidine (H), aspartic acid (D) and serine (S). Subtilisin E cleaves the bonds between hydrophobic and polar amino acids in keratin-associated proteins. The effects of point mutations on the crystal structure of subtilisin E (PDB ID: 1SCJ) showed that changes of asparagine 123 (N123) to valine (V) and serine 331 (S331) to leucine (L) respectively, were the most stabilizing. Genomic analysis of the subtilisin E-coding gene ( aprE ) indicated that this gene and the  yhfN  gene are expressed through a σA promoter. The analysis of TBFs revealed AbrB, ScoC, DegU, Hpr, σA, SinR, TenA, and DegU as relevant regulators of  aprE  expression. Phylogenetic analysis showed that subtilisin Es have highly conserved structures among  Bacillus  spp., sharing a common ancestor, where their coding genes were duplicated and evolved within the  Bacillus  spp. As the conclusion, our  in silico  study demonstrated that the overexpression of the  aprE  gene and stability of the produced subtilisin E can be improved though system biology methods such as point mutations and identifying the involved transcription factors (TFs) or/and TBFs. Communicated by Ramaswamy H. Sarma

Bioinformatics analysis of extracellular subtilisin E from Bacillus subtilis