Bacillus subtilis sequence

H Hemila, A Palva, L Paulin, S Arvidson, I Palva. Secretory complex of Bacillus subtilis. sequence analysis and identity to pyruvate dehydrogenase. J Bacteriol 172 5052-5063, 1990. 

In order to check whether the occurrence of the Rieske-type sequence motif is unique for the assimilatory nitrite reductase from Bacillus subtilis, the sequences of other assimilatory nitrite reductases were searched for the presence of the four putative ligands of Rieske-type clusters. A well-conserved sequence pattern... 

Structural analysis of the two pectate lyases PelC and PelE (5, 6), demonstrated that these proteins fold in a large heHx of parallel P strands. A stack of asparagine residues parallel to the helix probably plays a role in the stabUity of this structure. Identification of the structurally conserved amino adds lead to a reaHgnment of the protein sequences (7). In addition to Erwinia extracellular pectate lyases, the multiple aHgnment indudes the Bacillus subtilis pectate lyase, Aspergillus tdger and E. carotovora pectin lyases and plant proteins. 

The genes encoding the puc genes, which encode the enzymes in the aerobic pathway for the degradation of hypoxanthine, have been determined for Bacillus subtilis (Schultz et al. 2001), and involve the sequences (Figure 10.31) ... 

Figure 1. Amino acid sequences of microbial glycohydrolases. A Aureobasid-iwn sp. endo-xylanase Sc Schizophyllwn commune endo-xylanase C Chainia sp. endo-xylanase Bp Bacillus pumilus endo-xylanase Bs Bacillus subtilis Bacillus circulans endo-xylanase Pf Pseudomonas fluorescens endo-xylanase B alkalophilic Bacillus sp. endo-xylanase Ct Clostridium thermocellum endo-xylanase Cf Cellulomonas fimi cellobiohydrolase Ca Cryptococcus albidus endo-xylanase. Residue numbers are those of the adjacent residue, counting from the N-terminus of the mature protein.

The xylose isomerase DNA sequences from Bacillus subtilis (5), Escherichia coli (2,5), Streptomyces violaceoniger (4), and mAmpullariella sp., (6) were computer down-loaded from GenBank (Mountain View, CA). The sequence from Actinoplanes missouriensis (7) was typed into the computer twice. Discrepancies between the sequences were then compared to the original to produce a verified copy. Analysis of these sequences were performed using software developed by D. Mount and B. Conrad at the University of Arizona (Department of Molecular and Cellular Biology, Biosciences West, Tucson AZ). 

In 1998 the long-known Bacillus subtilis inorganic pyrophosphatase was characterized and found to have much greater activity than the above enzymes, to have a completely different amino acid sequence, not to be inhibited by F and to be activated by This form of... 

Kunst, F. Ogasawara, N, Moszer, I. et al The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature, 390, 249-256 (1997)... 

Lapidus, A. Galleron, N. Sorokin, A. Ehrlich, S.D. Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region. Microbiology, 143, 3431-3441 (1997)... 

Sorokin, A. Zumstein, E. Azevedo, V. Ehrlich, S.D. Serror, P. The organization of the Bacillus subtilis 168 chromosome region between the spo-VA and serA genetic loci, based on sequence data. Mol. Microbiol., 10, 385-395 (1993)... 

Trach, K.A. Hoch, J.A. Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis identification and sequence of the protein kinase of the alternate pathway. Mol. Microbiol., 8, 69-79 (1993)... 

The host bacteria used for production of recombinant proteins are usually E. coli, or Bacillus subtilis they may express proteins at 1 % to over 50% of the cellular protein, depending on such variables as the source, promoter structure, and vector type. Generally the proteins are expressed intracellularly, but leader sequences for excretion may be included. In the latter case, the protein is generally excreted into the periplasmic space, which limits the amount that can be produced. Excretion from grampositive species such as B. subtilis sends the product into the culture medium, with little feedback limitation on total expression level. 

Several amylases have been partially sequenced (42-45). For example, a-amylase from Bacillus subtilis, which is composed of two subunits of 24,000 molecular weight each, has an amino terminal sequence as shown in Table V (42). Perhaps fortuitously, the sequence of residues 8 through 12 resembles residues 14 through 18 in xylanase A, in that a polar residue is surrounded by four aromatic residues. 

Disaccharides analogous to sucrose, but having different rings might have useful biological properties. Galactosucrose was obtained by a multistep sequence from sucrose in 27% overall yield.235 An enzymatic route to this derivative, involving the fructosyltransferase (FTF) from Bacillus subtilis NCIMB... 

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