N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Bacillales: NE > Bacillaceae: NE > Bacillus: NE > Bacillus subtilis group: NE > Bacillus subtilis: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. Bacillus subtilis subsp. spizizenii ATCC 6633: N, E.
Bacillus subtilis subsp. spizizenii: N, E.
Bacillus subtilis BSn5: N, E.
Bacillus subtilis subsp. spizizenii str. W23: N, E.
Bacillus subtilis subsp. natto BEST195: N, E.
Bacillus subtilis subsp. subtilis str. 168: N, E.
Bacillus subtilis subsp. subtilis str. SC-8: N, E.
Bacillus subtilis subsp. spizizenii TU-B-10: N, E.
Bacillus subtilis subsp. subtilis str. RO-NN-1: N, E.
Bacillus subtilis QH-1: N, E.
Bacillus subtilis PY79: N, E.
Bacillus subtilis QB928: N, E.
Bacillus subtilis XF-1: N, E.
Bacillus subtilis subsp. subtilis str. BSP1: N, E.
Bacillus subtilis subsp. subtilis str. BAB-1: N, E.
Bacillus subtilis BEST7003: N, E.
Bacillus subtilis MB73/2: N, E.
Bacillus subtilis BEST7613: N, E.
Bacillus subtilis subsp. subtilis 6051-HGW: N, E.
Bacillus subtilis subsp. subtilis str. JH642 substr. AG174: N, E.
Bacillus subtilis subsp. subtilis str. AG1839: N, E.
Bacillus subtilis subsp. subtilis str. OH 131.1: N, E.
Bacillus subtilis E1: N, E.
Bacillus subtilis TO-A: N, E.
Bacillus subtilis Miyagi-4: N, E.
Bacillus subtilis subsp. subtilis: N, E.
Bacillus subtilis subsp. niger: N, E.
Bacillus subtilis subsp. inaquosorum KCTC 13429: 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 MRAERRKQLFRLLGDLPDRRPISVETLRIEEREENIVETLLLDLNGHEKA PAYFVKPKKTEGPCPAVLFQHSHGGQYDRGKSELIEGADYLKTPSFSDEL TSLGYGVLAIDHWGFGDRRGKAESEIFKEMLLTGKVMWGMMIYDSLSALD YMQSRSDVQPDRIGTIGMSMGGLMAWWTAALDDRIKVCVDLCSQVDHHVL IKTQNLDRHGFYYYVPSLAKHFSASEIQSLIAPRPHLSLVGVHDRLTPAE GVDKIEKELTAVYAGQGAADCYRVVRSASGHFETAVIRHEAVRFLQKWL
Bacillus subtilis is the best-characterized member of the Gram-positive bacteria. Its genome of 4,214,810 base pairs comprises 4,100 protein-coding genes. Of these protein-coding genes, 53% are represented once, while a quarter of the genome corresponds to several gene families that have been greatly expanded by gene duplication, the largest family containing 77 putative ATP-binding transport proteins. In addition, a large proportion of the genetic capacity is devoted to the utilization of a variety of carbon sources, including many plant-derived molecules. The identification of five signal peptidase genes, as well as several genes for components of the secretion apparatus, is important given the capacity of Bacillus strains to secrete large amounts of industrially important enzymes. Many of the genes are involved in the synthesis of secondary metabolites, including antibiotics, that are more typically associated with Streptomyces species. The genome contains at least ten prophages or remnants of prophages, indicating that bacteriophage infection has played an important evolutionary role in horizontal gene transfer, in particular in the propagation of bacterial pathogenesis.
A 10-kb region of the Bacillus subtilis genome that contains genes involved in biotin-biosynthesis was cloned and sequenced. DNA sequence analysis indicated that B. subtilis contains homologs of the Escherichia coli and Bacillus sphaericus bioA, bioB, bioD, and bioF genes. These four genes and a homolog of the B. sphaericus bioW gene are arranged in a single operon in the order bioWAFDR and are followed by two additional genes, bioI and orf2. bioI and orf2 show no similarity to any other known biotin biosynthetic genes. The bioI gene encodes a protein with similarity to cytochrome P-450s and was able to complement mutations in either bioC or bioH of E. coli. Mutations in bioI caused B. subtilis to grow poorly in the absence of biotin. The bradytroph phenotype of bioI mutants was overcome by pimelic acid, suggesting that the product of bioI functions at a step prior to pimelic acid synthesis. The B. subtilis bio operon is preceded by a putative vegetative promoter sequence and contains just downstream a region of dyad symmetry with homology to the bio regulatory region of B. sphaericus. Analysis of a bioW-lacZ translational fusion indicated that expression of the biotin operon is regulated by biotin and the B. subtilis birA gene.