The first structure of Bacillus licheniformis lipase BlEst2 in its propeptide and mature form revealing molecular details of inhibition by its C-terminal domains: Nakamura, A.M., Godoy, A.S., Kadowaki, M.A.S., Polikarpov, I. Other strains: DSM 13 / ATCC 14580; CG-B52
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Bacillaceae: NE > Bacillus: NE > Bacillus subtilis group: NE > Bacillus licheniformis: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Bacillus licheniformis ATCC 14580: N, E.
Bacillus licheniformis DSM 13 = ATCC 14580: N, E.
Bacillus licheniformis LMG 7559: N, E.
Bacillus licheniformis S 16: N, E.
Bacillus licheniformis WX-02: N, E.
Bacillus licheniformis CG-B52: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MKKLVLLMLVLLLVYPHVSKAGGFKGGGGNPGYWFAGDPVEHPDPAKPPI VFVHGLNGSSSAWFDENDMAEQAWKNGYDAAFIDLHPDKDMQDNGAMLAA KLREIYQYFGRKVILVSYSKGGIDSQSALIHHNAYHYVERVITLGTPHHG SQLADLAYSNWAGWLADILGQKNDAVYSLQTGFMKSFRDQTDNHPNRLKT KYFTLAGNKIGGFGSALFFGGVYLNMFGENDGAVTEKNARLPYATNLDTG KWDHFSIIKGNLTFPVFMPLLTIQANANETAATKENLSYPFIRGGENHGL REEEFAVEKGVKEITVHWLSNHSSGNIKLTDPRGKPFKDFSIAKTADVFE GGFVHSAAIKNPAAGTWKIASSVKQKEAFLFIVTFDSPLNQQIKNAVTRE SSNLANVKASVRSIRYENGKQAEKKSLKPASINALQNSLSFKKAGMYSVT IDLSGKTADNSPFNRTIIRSIYVNDKGEKFENSPLSD
BACKGROUND: Bacillus licheniformis is a Gram-positive, spore-forming soil bacterium that is used in the biotechnology industry to manufacture enzymes, antibiotics, biochemicals and consumer products. This species is closely related to the well studied model organism Bacillus subtilis, and produces an assortment of extracellular enzymes that may contribute to nutrient cycling in nature. RESULTS: We determined the complete nucleotide sequence of the B. licheniformis ATCC 14580 genome which comprises a circular chromosome of 4,222,336 base-pairs (bp) containing 4,208 predicted protein-coding genes with an average size of 873 bp, seven rRNA operons, and 72 tRNA genes. The B. licheniformis chromosome contains large regions that are colinear with the genomes of B. subtilis and Bacillus halodurans, and approximately 80% of the predicted B. licheniformis coding sequences have B. subtilis orthologs. CONCLUSIONS: Despite the unmistakable organizational similarities between the B. licheniformis and B. subtilis genomes, there are notable differences in the numbers and locations of prophages, transposable elements and a number of extracellular enzymes and secondary metabolic pathway operons that distinguish these species. Differences include a region of more than 80 kilobases (kb) that comprises a cluster of polyketide synthase genes and a second operon of 38 kb encoding plipastatin synthase enzymes that are absent in the B. licheniformis genome. The availability of a completed genome sequence for B. licheniformis should facilitate the design and construction of improved industrial strains and allow for comparative genomics and evolutionary studies within this group of Bacillaceae.
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.
Bacillus licheniformis lipase BlEst2 (EC 3.1.1.3)
