Description of Komagataeibacter gen. nov., with proposals of new combinations (Acetobacteraceae)

Yamada, Yoshihiko; Yukphan, Pattaraporn; Vu, Huong Thi; Muramatsu, Yuki; Ochaikul, Duangjai; Tanasupawat, Somboon; Nakagawa, Yasuyoshi

doi:10.2323/jgam.58.397

Cited by 264 publications

(145 citation statements)

References 22 publications

Supporting

Mentioning

129

Contrasting

Unclassified

Order By: Relevance

“…c-di-GMP was initially described (6) as an allosteric activator of cellulose biosynthesis in the alphaproteobacterium "Acetobacter xylinum" (also known as Gluconacetobacter xylinus and, more recently, Komagataeibacter xylinus [7]). The cellulose synthase (BCS) complex of K. xylinus includes four key subunits, referred to as BcsA, BcsB, BcsC, and BcsD, and fractionation of this complex mapped the c-di-GMP binding site to a 90-kDa BcsB-containing proteolytic fragment (8,9).…”

Section: Why More Than a Single C-di-gmp Adaptor Protein?mentioning

confidence: 99%

Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms

2016

View full text Add to dashboard Cite

Cyclic di-GMP (c-di-GMP) synthetases and hydrolases (GGDEF, EAL, and HD-GYP domains) can be readily identified in bacterial genome sequences by using standard bioinformatic tools. In contrast, identification of c-di-GMP receptors remains a difficult task, and the current list of experimentally characterized c-di-GMP-binding proteins is likely incomplete. Several classes of c-di-GMP-binding proteins have been structurally characterized; for some others, the binding sites have been identified; and for several potential c-di-GMP receptors, the binding sites remain to be determined. We present here a comparative structural analysis of c-di-GMP-protein complexes that aims to discern the common themes in the binding mechanisms that allow c-di-GMP receptors to bind it with (sub)micromolar affinities despite the 1,000-fold excess of GTP. The available structures show that most receptors use their Arg and Asp/Glu residues to bind c-di-GMP monomers, dimers, or tetramers with stacked guanine bases. The only exception is the EAL domains that bind c-di-GMP monomers in an extended conformation. We show that in c-di-GMPbinding signature motifs, Arg residues bind to the O-6 and N-7 atoms at the Hoogsteen edge of the guanine base, while Asp/Glu residues bind the N-1 and N-2 atoms at its Watson-Crick edge. In addition, Arg residues participate in stacking interactions with the guanine bases of c-di-GMP and the aromatic rings of Tyr and Phe residues. This may account for the presence of Arg residues in the active sites of every receptor protein that binds stacked c-di-GMP. We also discuss the implications of these structural data for the improved understanding of the c-di-GMP signaling mechanisms.

show abstract

Section: Why More Than a Single C-di-gmp Adaptor Protein?mentioning

confidence: 99%

Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms

2016

View full text Add to dashboard Cite

show abstract

“…Currently, apart from Acetobacter and Glu co nobacter, 17 other genera are classifi ed as AAB: Aci do monas, Ameyamaea, Asaia, Bombella, Commensalibacter, Endobacter, Gluconacetobacter, Granulibacter, Komagataeibacter, Kozakia, Neoasaia, Neokomagataea, Nguyenibacter, Saccharibacter, Swaminathania, Swingsia and Tanticharoenia (24). Diff erent vinegars show diff erent AAB profi les; nevertheless, species of the genera Acetobacter (25)(26)(27)(28), Gluconobacter (29,30) and Gluconacetobacter (31-33) (several of them have been recently renamed under the Komagataeibacter genus) (34) have been reportedly used in vinegar production.…”

Section: Introductionmentioning

confidence: 99%

Vinegar Production from Jabuticaba Fruits (Myrciaria jaboticaba) Using Immobilized Acetic Acid Bacteria

Dias

Silva

Souza

et al. 2016

Food Technol. Biotechnol.

View full text Add to dashboard Cite

SummaryCell immobilization comprises the retention of metabolically active cells inside a polymeric matrix. In this study, the production of jabuticaba (Myrciaria jaboticaba) vinegar using immobilized Acetobacter aceti and Gluconobacter oxydans cells is proposed as a new method to prevent losses of jabuticaba fruit surplus. The pulp of jabuticaba was processed and Saccharomyces cerevisiae CCMA 0200 was used to ferment the must for jabuticaba wine production. Sugars, alcohols (ethanol and glycerol) and organic acids were assayed by high-performance liquid chromatography. Volatile compounds were determined by gas chromatography-fl ame ionization detector. The ethanol content of the produced jabuticaba wine was approx. 74.8 g/L (9.5 % by volume) aft er 168 h of fermentation. Acetic acid fermentation for vinegar production was performed using a mixed culture of immobilized A. aceti CCT 0190 and G. oxydans CCMA 0350 cells. The acetic acid yield was 74.4 % and productivity was 0.29 g/(L·h). The vinegar had particularly high concentrations of citric (6.67 g/L), malic (7.02 g/L) and succinic (5.60 g/L) acids. These organic acids give a suitable taste and fl avour to the vinegar. Seventeen compounds (aldehydes, higher alcohols, terpene, acetate, diether, furans, acids, ketones and ethyl esters) were identifi ed in the jabuticaba vinegar. In conclusion, vinegar was successfully produced from jabuticaba fruits using yeast and immobilized mixed cultures of A. aceti and G. oxydans. To the best of our knowledge, this is the fi rst study to use mixed culture of immobilized cells for the production of jabuticaba vinegar.

show abstract

“…Strains assigned to the genus Komagataeibacter were mostly isolated from acetous or sugary materials such as vinegar, konnyaku (cellulosic materials formed during vinegar production), kombucha, fruit and fruit juice. At the time of writing, there were eleven species with validly published names accommodated in the genus Komagataeibacter (Yamada et al, 2012b(Yamada et al, , 2013. However, Gluconacetobacter entanii was not listed in the genus Komagataeibacter, since the type strain of this species is not available in any culture collections including the DSMZ (Schüller et al, 2000;Yamada et al, 2012b).…”

mentioning

confidence: 99%

Transfer of Gluconacetobacter kakiaceti, Gluconacetobacter medellinensis and Gluconacetobacter maltaceti to the genus Komagataeibacter as Komagataeibacter kakiaceti comb. nov., Komagataeibacter medellinensis comb. nov. and Komagataeibacter maltaceti comb. nov.

Yamada

2014

International Journal of Systematic and Evolutionary Microbiology

Self Cite

View full text Add to dashboard Cite

Gluconacetobacter kakiaceti , Gluconacetobacter medellinensis and Gluconacetobacter maltaceti are transferred to the genus Komagataeibacter as Komagataeibacter kakiaceti comb. nov. (type strain, G5-1T = JCM 25156T = NRIC 0798T = LMG 26206T), Komagataeibacter medellinensis comb. nov. (type strain, LMG 1693T = NBRC 3288T = Kondo 51T) and Komagataeibacter maltaceti comb. nov. (type strain, LMG 1529T = NBRC 14815T = NCIMB 8752T).

show abstract

Description of Komagataeibacter gen. nov., with proposals of new combinations (Acetobacteraceae)

Cited by 264 publications

References 22 publications

Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms

Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms

Vinegar Production from Jabuticaba Fruits (Myrciaria jaboticaba) Using Immobilized Acetic Acid Bacteria

Transfer of Gluconacetobacter kakiaceti, Gluconacetobacter medellinensis and Gluconacetobacter maltaceti to the genus Komagataeibacter as Komagataeibacter kakiaceti comb. nov., Komagataeibacter medellinensis comb. nov. and Komagataeibacter maltaceti comb. nov.

Contact Info

Product

Resources

About