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Background  Sublancin is a novel and distinct antimicrobial glycopeptide that can be used as an alternative to conventional antibiotics. The reported production of sublancin by  Bacillus subtilis  168 is poor because transcriptional regulatory circuit of  sunA , a gene that encodes presublancin, is complex and difficult to control.    Results  A strong inducible and easy to control vegetative σ A  promoter of P  glv   was introduced to replace that of  sunA in situ  in  B. subtilis  1A747 [SPβc, prototroph, the derivative of  B. subtilis  168 (trpC2)]. Meanwhile, other two strong promoters of P43 and P  luxS   were respectively placed before  sunI  and  sunT – bdbA – sunS – bdbB , encoding five functional proteins that involved in the biosynthesis of mature sublancin. 642 mg sublancin was obtained from 1 L culture supernatant of recombinant  B. subtilis  1A747 strains. Analysises of electrospray ionization mass spectrometry and circular dichroism spectrum showed that mature sublancin had a molecular weight of 3877.642 Da and displayed a α–helical conformation that are consistent with reported results. In addition, the mature sublancin was proved to be a potent antimicrobial glycopeptide with broad activity spectrum, moderate cytotoxicity and good conditional stability under high temperature, extreme pH and protease–rich environments, thus showing its potential for clinical applications.    Conclusions  Our present findings suggest that recombinant  B. subtilis  1A747 strains can effectively and efficiently biosynthesize mature sublancin. The replacement of native promoters provides an extra method for production improvement of some other complicated peptides such as nisin and subtilin.    Electronic supplementary material  The online version of this article (doi:10.1186/s12934-015-0201-0) contains supplementary material, which is available to authorized users.

microbial cell factories

Improved production of sublancin via introduction of three characteristic promoters into operon clusters responsible for this novel distinct glycopeptide biosynthesis