Exemplar Abstract for Anoxybacillus flavithermus flavithermus (Pikuta et al. 2000) Dai et al. 2011 and Anoxybacillus flavithermus Pikuta et al. 2000.

ABSTRACTFree ions of Na+, K+, Ca2+, and Mg2+influenced the optical density of planktonic cultures of thermophilic bacilli.Anoxybacillus flavithermusE16 andGeobacillussp. strain F75 (milk powder manufacturing plant isolates) andA. flavithermusDSM 2641 andG. thermoleovoransDSM 5366 were studied. Ca2+and Mg2+were associated with increases in optical density more so than Na+and K+. Overall, it appeared that Ca2+and/or Mg2+was required for the production of protein in thermophilic bacilli, as shown by results obtained withA. flavithermusE16, which was selected for further study.

Download Full-text

Draft genome sequence of Anoxybacillus flavithermus KU2-6-11 isolated from hot-spring in Uzon caldera (Kamchatka, Russia)

Data in Brief ◽

10.1016/j.dib.2017.11.095 ◽

2018 ◽

Vol 16 ◽

pp. 758-761

Author(s):

Aleksey S. Rozanov ◽

Anton V. Korzhuk ◽

Alla V. Bryanskaya ◽

Sergey E. Peltek

Keyword(s):

Genome Sequence ◽

Hot Spring ◽

Draft Genome ◽

Draft Genome Sequence ◽

Uzon Caldera ◽

Anoxybacillus Flavithermus

Download Full-text

Draft Genome Sequence of a Thermophilic Member of the Bacillaceae, Anoxybacillus flavithermus Strain Kn10, Isolated from the Kan-nawa Hot Spring in Japan

Genome Announcements ◽

10.1128/genomea.00311-13 ◽

2013 ◽

Vol 1 (3) ◽

Cited By ~ 6

Author(s):

M. Matsutani ◽

Y. Shirakihara ◽

K. Imada ◽

T. Yakushi ◽

K. Matsushita

Keyword(s):

Genome Sequence ◽

Hot Spring ◽

Draft Genome ◽

Draft Genome Sequence ◽

Anoxybacillus Flavithermus

Download Full-text

Isolation of a thermophilic Anoxybacillus flavithermus sp. nov. and production of thermostable α-amylase under solid-state fermentation (SSF)

Annals of Microbiology ◽

10.1007/s13213-011-0385-4 ◽

2011 ◽

Vol 62 (4) ◽

pp. 1367-1375 ◽

Cited By ~ 10

Author(s):

Sadin Özdemir ◽

Fatma Matpan ◽

Veysi Okumus ◽

Abdurrahman Dündar ◽

Mehmet Sefa Ulutas ◽

...

Keyword(s):

Solid State ◽

Solid State Fermentation ◽

Anoxybacillus Flavithermus

Download Full-text

Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter

eLife ◽

10.7554/elife.59407 ◽

2020 ◽

Vol 9 ◽

Cited By ~ 4

Author(s):

Julia Steiner ◽

Leonid Sazanov

Keyword(s):

Electron Transfer ◽

Electrostatic Interactions ◽

Proton Translocation ◽

Proton Pumps ◽

Entire Family ◽

Surface Charge Distribution ◽

Large Protein Family ◽

Anoxybacillus Flavithermus ◽

Respiratory Complex I ◽

Ph Adaptation

Multiple resistance and pH adaptation (Mrp) antiporters are multi-subunit Na+ (or K+)/H+ exchangers representing an ancestor of many essential redox-driven proton pumps, such as respiratory complex I. The mechanism of coupling between ion or electron transfer and proton translocation in this large protein family is unknown. Here, we present the structure of the Mrp complex from Anoxybacillus flavithermus solved by cryo-EM at 3.0 Å resolution. It is a dimer of seven-subunit protomers with 50 trans-membrane helices each. Surface charge distribution within each monomer is remarkably asymmetric, revealing probable proton and sodium translocation pathways. On the basis of the structure we propose a mechanism where the coupling between sodium and proton translocation is facilitated by a series of electrostatic interactions between a cation and key charged residues. This mechanism is likely to be applicable to the entire family of redox proton pumps, where electron transfer to substrates replaces cation movements.

Download Full-text