(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 subtilis: 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 subtilis subsp. spizizenii ATCC 6633: N, E.
Bacillus subtilis subsp. spizizenii: N, E.
Bacillus subtilis subsp. natto BEST195: N, E.
Bacillus subtilis subsp. spizizenii str. W23: N, E.
Bacillus subtilis BSn5: N, E.
Bacillus subtilis QH-1: N, E.
Bacillus subtilis QB928: N, E.
Bacillus subtilis subsp. subtilis str. BAB-1: N, E.
Bacillus subtilis BEST7613: N, E.
Bacillus subtilis subsp. subtilis str. SC-8: N, E.
Bacillus subtilis MB73/2: N, E.
Bacillus subtilis BEST7003: N, E.
Bacillus subtilis XF-1: N, E.
Bacillus subtilis subsp. spizizenii TU-B-10: N, E.
Bacillus subtilis subsp. subtilis str. 168: N, E.
Bacillus subtilis subsp. subtilis str. RO-NN-1: N, E.
Bacillus subtilis PY79: N, E.
Bacillus subtilis subsp. subtilis str. BSP1: 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.
Bacillus subtilis subsp. globigii: N, E.
Bacillus halotolerans: 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 ENRQDLTPPRNWVEQELTQIWKSVLGVKTIGIHDDFFALGGHSLKALQVI HMLKHHQHVDIPIDVLFENPTIAQLAEKLYSNQLSAAGEQHVIQLNQQGG KNLFCFPPISGFGIYFKDLALQLNHKAAVYGFHFIEEDSRIEQYVSRITE IQPEGPYVLLGYSAGGNLAFEVVQAMEQKGLEVSDFIIVDAYKKDQSITA DTENDDSAAYLPEAVRETVMQKKRCYQEYWAQLINEGRIKSNIHFIEAGI QTETSGAMVLQKWQDAAEEGYAEYTGYGAHKDMLEGEFAEKNANIILNIL DKINSDQKVLPNKH
References
Title: The thioesterase domain of the fengycin biosynthesis cluster: a structural base for the macrocyclization of a non-ribosomal lipopeptide Samel SA, Wagner B, Marahiel MA, Essen LO Ref: Journal of Molecular Biology, 359:876, 2006 : PubMed
Many secondary metabolic peptides from bacteria and fungi are produced by non-ribosomal peptide synthetases (NRPS) where the final step of biosynthesis is often catalysed by designated thioesterase domains. Here, we report the 1.8A crystal structure of the fengycin thioesterase (FenTE) from Bacillus subtilis F29-3, which catalyses the regio- and stereoselective release and macrocyclization of the antibiotic fengycin from the NRPS template. A structure of the PMSF-inactivated FenTE domain suggests the location of the oxyanion hole and the binding site of the C-terminal residue l-Ile11 of the lipopeptide. Using a combination of docking, molecular dynamics simulations and in vitro activity assays, a model of the FenTE-fengycin complex was derived in which peptide cyclization requires strategic interactions with residues lining the active site canyon.
Title: Transposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis. Chen CL, Chang LK, Chang YS, Liu ST, Tschen JS Ref: Molecular & General Genetics, 248:121, 1995 : PubMed
Bacillus subtilis; Bacillus malacitensis; Bacillus [Brevibacterium] halotolerans fengycin synthetase
