The Complete Genome Sequence of  Bacillus licheniformis DSM13, an Organism with Great Industrial Potential | Zendy

Birgit Veith | Zendy; Christina Herzberg | Zendy; Silke Steckel | Zendy; Jörg Feesche | Zendy; Karl Heinz Maurer | Zendy; Petra Ehrenreich | Zendy; Sebastian Bäumer | Zendy; Anke Henne | Zendy; Heiko Liesegang | Zendy; Rainer Merkl | Zendy; Armin Ehrenreich | Zendy; Gerhard Gottschalk | Zendy

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The Complete Genome Sequence of <i> Bacillus licheniformis </i>DSM13, an Organism with Great Industrial Potential

Author(s) -

Birgit Veith,

Christina Herzberg,

Silke Steckel,

Jörg Feesche,

Karl Heinz Maurer,

Petra Ehrenreich,

Sebastian Bäumer,

Anke Henne,

Heiko Liesegang,

Rainer Merkl,

Armin Ehrenreich,

Gerhard Gottschalk

Publication year - 2004

Publication title -

microbial physiology

Language(s) - English

Resource type - Journals

eISSN - 2673-1673

pISSN - 2673-1665

DOI - 10.1159/000079829

Subject(s) - bacillus licheniformis , biology , gene , genome , prophage , operon , bacillus subtilis , genetics , escherichia coli , bacteria , bacteriophage

The genome of Bacillus licheniformis DSM13 consists of a single chromosome that has a size of 4,222,748 base pairs. The average G+C ratio is 46.2%. 4,286 open reading frames, 72 tRNA genes, 7 rRNA operons and 20 transposase genes were identified. The genome shows a marked co-linearity with Bacillus subtilis but contains defined inserted regions that can be identified at the sequence as well as at the functional level. B. licheniformis DSM13 has a well-conserved secretory system, no polyketide biosynthesis, but is able to form the lipopeptide lichenysin. From the further analysis of the genome sequence, we identified conserved regulatory DNA motives, the occurrence of the glyoxylate bypass and the presence of anaerobic ribonucleotide reductase explaining that B. licheniformis is able to grow on acetate and 2,3-butanediol as well as anaerobically on glucose. Many new genes of potential interest for biotechnological applications were found in B. licheniformis; candidates include proteases, pectate lyases, lipases and various polysaccharide degrading enzymes.

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