نتایج جستجو برای: bacillus subtilis 168

تعداد نتایج: 69117  

Journal: :Antimicrobial agents and chemotherapy 2005
Kenji Tsuge Satoka Inoue Takashi Ano Mitsuhiro Itaya Makoto Shoda

Iturin A and its derivatives are lipopeptide antibiotics produced by Bacillus subtilis and several closely related bacteria. Three iturin group operons (i.e., iturin A, mycosubtilin, and bacillomycin D) of those antibiotic-producing strains have been cloned and sequenced thus far, strongly implying the horizontal transfer of these operons. To examine the nature of such horizontal transfer in te...

2014
Chantal V. Garcia De Gonzalo Lingyang Zhu Trent J. Oman Wilfred A. van der Donk

Sublancin 168 is a member of a small group of glycosylated antimicrobial peptides known as glycocins. The solution structure of sublancin 168, a 37-amino-acid peptide produced by Bacillus subtilis 168, has been solved by nuclear magnetic resonance (NMR) spectroscopy. Sublancin comprises two α-helices and a well-defined interhelical loop. The two helices span residues 6-16 and 26-35, and the loo...

2016
Erwin M. Berendsen Rosella A. Koning Jos Boekhorst Anne de Jong Oscar P. Kuipers Marjon H. J. Wells-Bennik

Bacterial endospore formers can produce spores that are resistant to many food processing conditions, including heat. Some spores may survive heating processes aimed at production of commercially sterile foods. Recently, it was shown that a spoVA operon, designated spoVA2mob, present on a Tn1546 transposon in Bacillus subtilis, leads to profoundly increased wet heat resistance of B. subtilis sp...

Journal: :Antimicrobial agents and chemotherapy 2001
K Tsuge Y Ohata M Shoda

Surfactin is a cyclic lipopeptide biosurfactant. Transposon mutagenesis was performed in Bacillus subtilis strain 168, and a surfactin-susceptible mutant, strain 801, was isolated. Analysis of the region of insertion revealed that yerP was the determinant of surfactin self-resistance. YerP had homology with the resistance, nodulation, and cell division (RND) family proton motive force-dependent...

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