Alkaliphilic Bacterium Research Articles

Bacteria with industrial potential from Lake Nakuru, Kenya

Bacteria with industrial potential in Lake Nakuru were isolated and characterised over six months in 2010. The enzymatic activities of 30 isolates towards various macromolecules were investigated by testing their ability to degrade starch, cellulose, casein and lipid substrates. Fifteen isolates exhibited an ability to degrade macromolecules, with some able to hydrolyse two or more macromolecules, including 8 degrading starch, 6 proteins, 5 cellulose and 5 lipids. The genomic DNA of the LNS08, LNC09, LNC11 and LNC06 isolates, which showed the highest potential to degrade macromolecules, were analysed and their identity closely related to the known bacteria Nesterenkonia lacusekhoensis (LNS08), Bacillus agaradhaerens (LNC06) and Bacillus sp. accession no. AB043860.1 (LNC09 and LNC11). Nesterenkonia lacusekhoensis can be used as a lipid degrader, B. agaradhaerens can be used in the degradation of proteins and Bacillus sp. accession no. AB043860.1 has potential for the production of sugars from starch and cellulose. Lake Nakuru is thus a rich source of alkaliphilic bacteria that can be used in industry.

Crystallization and preliminary X-ray diffraction analysis of the arginine repressor ArgR from Bacillus halodurans.

The arginine repressor (ArgR) is a transcriptional regulator which regulates genes encoding proteins involved in arginine biosynthesis and the arginine catabolic pathway. ArgR from the alkaliphilic bacterium Bacillus halodurans was cloned and overexpressed in Escherichia coli. ArgR (Bh2777) from B. halodurans is composed of 149 amino-acid residues with a molecular mass of 16 836 Da. ArgR was crystallized at 296 K using 1,2-propanediol as a precipitant. Crystals of N-terminally His-tagged ArgR were obtained by the sitting-drop vapour-diffusion method. Dehydrated crystals showed a dramatic improvement in diffraction quality and diffracted to 2.35 Å resolution. The crystals belonged to the cubic space group I23, with unit-cell parameters a = b = c = 104.68 Å. The asymmetric unit contained one monomer of ArgR, which generates a trimer by the threefold axis of the space group, giving a crystal volume per mass (VM) of 2.98 Å(3) Da(-1) and a solvent content of 56.8%.

好アルカリ性細菌のエネルギー代謝機構から見たチトクロム<i>c</i>の多機能

好アルカリ性細菌のエネルギー代謝機構から見たチトクロム<i>c</i>の多機能

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

Nitro aromatic compounds are the potential toxic organic pollutant released into the environment and are often resistant to degradation under normal environmental conditions. The biotransformation and/or detoxification of these compounds can be possible by microbial azoreductase enzyme. Azoreductase enzyme has an ability to reduce the toxic nitro group to corresponding amino group. In present report, the flavin-free NADH azoreductase was isolated and purified from alkaliphilic bacteria Bacillus badius. The enzyme was purified by a combination of ammonium sulphate precipitation and size exclusion chromatography. The purified azoreductase has efficiently demonstrated both azoreductase and nitroreductase activities. The biochemical properties of the azoreductase including cofactor requirement, substrate specificity and enzyme inhibition have been studied. The biotransformation of some selected nitro aromatic compounds like 3-nitro benzoic acid, 4-nitro toluene, 3-nitro toluene and 1-chloro-2-nitro benzene by purified azoreductase was carried out at 37°C. The reduction products of these nitro aromatic compounds were analyzed by IR and NMR spectroscopy.

Gene cloning and enzymatic characterization of alkali-tolerant type I pullulanase from Exiguobacterium acetylicum.

A pullulanase gene (Pul3YH5) of 2568bp, which encodes a protein containing 855 amino acid residues, was cloned from the alkaliphilic bacterium Exiguobacterium acetylicum YH5. The pullulanase (Pul3YH5) contains the YNWGYDP motif of type I pullulanase as well as four conserved glycoside hydrolase sequences of the GH13 (α-amylase) family. When the pullulanase gene was cloned and expressed in Escherichia coli BL21 (DE3) plysS, the recombinant pullulanase had a molecular mass of ˜100·0kDa. It was optimally active at 50°C and pH 6·0, alkali-tolerant and displayed excellent stability (>93·0%) over a broad pH range (4·0-10·0) when incubated for 30min without substrate. The enzyme activity of Pul3YH5 was significantly enhanced in the presence of Co(2+) , Fe(2+) and Mn(2+) and was inhibited by Cu(2+) , SDS, β-mercaptoethanol and EDTA. The enzyme displayed the highest specificity forpullulan (Km =0·12±0·02mgml(-1) ), followed by soluble starch (Km = 0·69±0·04mgml(-1) ). Substrate hydrolysis demonstrated that pullulanase from E.acetylicum liberated maltotriose from pullulan, although hydrolytic activity was also detected with soluble starch, amylopectin, β-limited dextrin and glycogen. These enzymatic properties indicate that Pul3YH5 is alkali-tolerant pullulanase and that Pul3YH5 could be useful in the detergent industry. Pullulanases have great potential in various industries, ranging from food (high fructose and glucose syrups) to washing detergent industries. In this study, the gene encoding the novel pullulanase from E.acetylicum YH5 was cloned and sequenced, then expressed in E.coli. The properties of the recombinant enzyme in E.coli were also determined. The pullulanase from E.acetylicum YH5 is alkaline tolerant and has a high optimum temperature, making it a candidate for applications in the detergent industry.

Draft Genome Sequence of the Obligately Alkaliphilic Sulfate-Reducing Bacterium Desulfonatronum thiodismutans Strain MLF1.

Desulfonatronum thiodismutans strain MLF1, an alkaliphilic bacterium capable of sulfate reduction, was isolated from Mono Lake, California. Here we report the 3.92-Mb draft genome sequence comprising 34 contigs and some results of its automated annotation. These data will improve our knowledge of mechanisms by which bacteria withstand extreme environments.

Salinispirillum marinum gen. nov., sp. nov., a haloalkaliphilic bacterium in the family 'Saccharospirillaceae'.

A novel Gram-staining-negative, motile, non-pigmented, facultatively anaerobic, spirillum-shaped, halophilic and alkaliphilic bacterium, designated strain GCWy1(T), was isolated from water of the coastal-marine wetland Gomishan in Iran. The strain was able to grow at NaCl concentrations of 1-10% (w/v) and optimal growth was achieved at 3% (w/v). The optimum pH and temperature for growth were pH 8.5 and 30 °C, while the strain was able to grow at pH 7.5-10 and 4-40 °C. Phylogenetic analysis based on the comparison of the 16S rRNA gene sequence placed the isolate within the class Gammaproteobacteria as a separate deep branch, with 92.1% or lower sequence similarity to representatives of the genera Saccharospirillum and Reinekea and less than 91.0% sequence similarity with other remotely related genera. The major cellular fatty acids of the isolate were C(18 : 1)ω7c, C(16:0) and C(17 : 0), and the major components of its polar lipid profile were diphosphatidylglycerol, phosphatidylglycerol and phosphatidylethanolamine. The cells of strain GCWy1(T) contained the isoprenoid quinones Q-9 and Q-8 (81% and 2%, respectively). The G+C content of the genomic DNA of this strain was 52.3 mol%. On the basis of 16S rRNA gene sequence analysis in combination with chemotaxonomic and phenotypic data, strain GCWy1(T) represents a novel species in a new genus in the family 'Saccharospirillaceae', order Oceanospirillales, for which the name Salinispirillum marinum gen. nov., sp. nov. is proposed. The type strain of the type species is GCWy1(T) ( = IBRC-M 10765(T) =CECT 8342(T)).

Biological neutralization and biosorption of dyes of alkaline textile industry wastewater

The present work was aimed to secure biological neutralization and biosorption of dyes of an alkaline textile industrial effluent (ATIE) using an alkaliphilic bacterium, Enterococcus faecalis strain R-16 isolated from Gujarat coast. The isolate was capable and competent to bring down the pH of ATIE from 12.1 to 7.0 within 2h in the presence of carbon and nitrogen sources. Carboxylic group concentration (CGC), NMR and FT-IR analysis revealed production of carboxylic acid as a result of neutralization. The unconventional carbon and nitrogen sources like Madhuca indica flowers or sugar cane bagasse supported the growth of bacterium with effective neutralization and biosorption of dyes from ATIE. The process proved to be efficient, inexpensive and eco-friendly as compared to conventional chemical neutralization process.

Bacillus fengqiuensis sp. nov., isolated from a typical sandy loam soil under long-term fertilization.

A Gram-staining-positive, endospore-forming, moderately alkaliphilic bacterium, strain NPK15(T), was isolated from a typical sandy loam soil under long-term NPK fertilization in northern China and was subjected to a polyphasic taxonomic study. The diamino acid of the cell-wall peptidoglycan of strain NPK15(T) was found to be meso-diaminopimelic acid and the cell-wall sugars were xylose, glucose and traces of mannose. The only respiratory quinone found in strain NPK15(T) was menaquinone 7 (MK-7). The major cellular fatty acids were iso-C(15 : 0), anteiso-C(15 : 0), C(16 : 0) and C(16 : 1)ω6c/C(16 : 1)ω7c. The major polar lipids were diphosphatidylglycerol, phosphatidylethanolamine and phosphatidylglycerol. Phylogenetic analysis of the strain based on its 16S rRNA gene sequence showed that it was related most closely to 'Bacillus thaonhiensis' KACC 17216 (99.59%), B. songklensis KCTC 13881(T) (99.52%) and B. abyssalis CCTCC AB 2012074(T) (99.00%). DNA-DNA hybridization results indicated that the strain was distinct from other species of the genus Bacillus, the degree of relatedness being 35.4% with B. abyssalis CCTCC AB 2012074(T), 39.7% with B. songklensis KCTC 13881(T) and 51.2% with 'B. thaonhiensis' KACC 17216. The DNA G+C content of strain NPK15(T) was 45.5 mol%. Phenotypic, chemotaxonomic and molecular analyses identified strain NPK15(T) as a member of a novel species of the genus Bacillus, for which the name Bacillus fengqiuensis sp. nov. is proposed. The type strain is NPK15(T) ( = DSM 26745(T) = CCTCC AB 2013156(T)).

Bacillus alkalicola sp. nov., an alkaliphilic, gram-positive bacterium isolated from Zhabuye Lake in Tibet, China.

A Gram-positive, alkaliphilic bacterium, designated strain Zby6(T), was isolated from Zhabuye Lake in Tibet, China. The strain was able to grow at pH 8.0-11.0 (optimum at pH 10.0), in 0-8 % (w/v) NaCl (optimum at 3 %, w/v) and at 10-45 °C (optimum at 37 °C). Cells of the isolate were facultatively anaerobic and spore-forming rods with polar flagellum. The predominant isoprenoid quinone was MK-7, and its cell wall peptidoglycan contained meso-diaminopimelic acid. The major cellular fatty acids were iso-C(15:0), C(16:0) and anteiso-C(15:0). The major polar lipids consisted of phosphatidylglycerol, diphosphatidylglycerol, and phosphatidylethanolamine. The genomic DNA G+C content of the isolate was 38.9 mol%. Phylogenetic analysis based on 16S rRNA gene sequences revealed that strain Zby6(T) was a member of the genus Bacillus and most closely related to Bacillus cellulosilyticus DSM 2522(T) (97.7 % similarity). The DNA-DNA relatedness value between strain Zby6(T) and B. cellulosilyticus DSM 2522(T) was 59.2 ± 1.8 %. Comparative analysis of genotypic and phenotypic features indicated that strain Zby6(T) represents a novel species of the genus Bacillus, for which the name Bacillus alkalicola sp. nov. is proposed; the type strain is Zby6(T) (=CGMCC 1.10368(T) = JCM 17098(T) = NBRC 107743(T)).

Cardiolipin Is Dispensable for Oxidative Phosphorylation and Non-fermentative Growth of Alkaliphilic Bacillus pseudofirmus OF4

Cardiolipin (CL), a membrane phospholipid in bacteria and mitochondria, has been hypothesized to facilitate movement of protons on the outer surface of membranes in support of respiration-dependent ATP synthesis, oxidative phosphorylation (OXPHOS). If so, the high levels of membrane CL found in alkaliphilic bacteria, such as Bacillus pseudofirmus OF4, might facilitate its robust OXPHOS at pH 10.5, where the bulk protonmotive (PMF) force is low. To address the role of CL in Bacillus pseudofirmus OF4, we studied strains in which genes (cls) potentially encoding a CL synthase (CLs) were deleted: three single (ΔclsA, ΔclsB, and ΔclsC), one double (ΔclsA/B), and one triple (ΔclsA/B/C) mutant. Two-dimensional thin layer chromatography analyses of lipid extracts from (32)P-labeled strains showed that the wild-type CL content was 15% of total phospholipids at pH 10.5 versus 3% at pH 7.5 during log phase. The % CL was higher (28-33%) at both pH values during stationary phase. The clsA gene plays a major role in CL biosynthesis as no detectable CL was found in ΔclsA-containing mutants, whereas the CL precursor phosphatidylglycerol was elevated. The ΔclsB mutant exhibited no significant reduction in CL, but clsB expression was up-regulated and appeared to support growth at pH 7.5. In the absence of detectable CL, the alkaliphile showed no significant deficits in non-fermentative growth, respiration-dependent ATP synthesis, or salt tolerance. Minor deficits in respiration and ATP synthase assembly were noted in individual mutants. In long term survival experiments, significant growth defects were found in ΔclsA strains and the ΔclsC strain at pH 10.5.

Isolation of Cytochrome P-450cam from Alkaliphilic bacteriaKocuria sp. DL

Cytochrome P-450 is a terminal oxidase, involved in biotransformation of endogenous and exogenous substances. Cytochrome P-450cam is isozyme present in various bacteria. CYP-450cam was purified from alkaliphilic bacteria, Kocuria sp. DL, isolated from pristine alkaline Crater Lake, Lonar, (Maharashtra State), India. Identification of this bacterial strain was carried out by analysis of 16S rRNA gene sequence (Kocuria species DL strain). The content of CYP-450cam was found to be 2.68 n mol/mg of protein in 50 h grown culture under aerobic condition. Purification of CYP-450cam was carried out by applying analytical procedures at 4 oC. The Km values for both aminopyrine and acetanilide were 0.4 and 0.25 mM, respectively. The maximal velocity Vmax was 12.98 and 13.2 mM/mg of protein per min for aminopyrine and acetanilide, respectively. The optimal pH and temperatures were found to be 7.4 and 40 oC, respectively. The purification fold was found to be 6. The molecular mass was found to be 48 kDa. Thermal stability of purified CYP-450cam is up to 40 oC. This enzyme has shown the characteristic type-I and type-II substrate binding spectra.

Isolation of alkaliphilic bacteria for production of high optically pure L-(+)-lactic acid.

Lactic acid bacteria that grow under alkaline conditions (pH 10) were isolated from various sources in Okinawa (Japan). These alkali-tolerant and alkaliphilic bacteria were classified as follows: Microbacterium sp. (1 strain), Enterococcus spp. (9 strains), Alkalibacterium spp. (3 strains), Exiguobacterium spp. (5strains), Oceanobacillus spp. (3 strains) and Bacillus spp. (7 strains) by 16S rRNA gene sequencing. By fermentation, many strains were able to convert glucose into mainly L-(+)-lactic acid of high optical purity in alkaline broth. This result indicated that valuable L-(+)-lactic acid-producing bacteria could be isolated efficiently by screening under alkaline conditions. Six strains were selected and their ability to produce lactic acid at different initial pH was compared. Enterococcus casseliflavus strain 79w3 gave the highest lactic acid concentration. Lactic acid concentration and productivity were 103 g L(-1) (optical purity of 99.5% as L-isomer) and 2.2 g L(-1) h(-1), respectively when 129 g L(-1) of glucose was used by batch fermentation.

New Insights into the Phylogeny and Molecular Classification of Nicotinamide Mononucleotide Deamidases

Nicotinamide mononucleotide (NMN) deamidase is one of the key enzymes of the bacterial pyridine nucleotide cycle (PNC). It catalyzes the conversion of NMN to nicotinic acid mononucleotide, which is later converted to NAD+ by entering the Preiss-Handler pathway. However, very few biochemical data are available regarding this enzyme. This paper represents the first complete molecular characterization of a novel NMN deamidase from the halotolerant and alkaliphilic bacterium Oceanobacillus iheyensis (OiPncC). The enzyme was active over a broad pH range, with an optimum at pH 7.4, whilst maintaining 90 % activity at pH 10.0. Surprisingly, the enzyme was quite stable at such basic pH, maintaining 61 % activity after 21 days. As regard temperature, it had an optimum at 65 °C but its stability was better below 50 °C. OiPncC was a Michaelian enzyme towards its only substrate NMN, with a K m value of 0.18 mM and a kcat/K m of 2.1 mM-1 s-1. To further our understanding of these enzymes, a complete phylogenetic and structural analysis was carried out taking into account the two Pfam domains usually associated with them (MocF and CinA). This analysis sheds light on the evolution of NMN deamidases, and enables the classification of NMN deamidases into 12 different subgroups, pointing to a novel domain architecture never before described. Using a Logo representation, conserved blocks were determined, providing new insights on the crucial residues involved in the binding and catalysis of both CinA and MocF domains. The analysis of these conserved blocks within new protein sequences could permit the more efficient data curation of incoming NMN deamidases.

A new low molecular mass alkaline cyclodextrin glucanotransferase from Amphibacillus sp. NRC-WN isolated from an Egyptian soda lake

Background: Cyclodextrin glucanotransferase (CGTase) is one of the most industrially important enzymes used in the commercial production of cyclodextrins (CDs). Alkaliphilic bacteria have attracted much interest in the last few decades because of their ability to produce extracellular enzymes that are active and stable at high pH values. Here, we report the isolation of a new CGTase from alkaliphilic bacteria collected from Egyptian soda lakes and describe the purification and biochemical characterization of this CGTase. Results: Screening for CGTase-producing alkaliphilic bacteria from sediment and water samples collected from Egyptian soda lakes located in the Wadi Natrun valley resulted in the isolation of a potent CGTase-producing alkaliphilic bacterial strain, designated NRC-WN. Strain NRC-WN was belonging to genus Amplibacullus by 16S rDNA sequence analysis (similarity: ca. 98%). Among the tested nitrogen and carbon sources, peptone (0.15%, w/v) and soluble starch (0.4%, w/v) allowed maximal CGTase production by Amphibacillus sp. NRC-WN. CGTase was successfully purified from Amphibacillus sp. NRC-WN up to 159.7-fold through a combination of starch adsorption and anion exchange chromatography, resulting in a yield of 84.7%. SDS-PAGE analysis indicated that the enzyme was purified to homogeneity and revealed an estimated molecular mass of 36 kDa, which makes it one of the smallest CGTases reported in the literature. The purified enzyme exhibited maximum activity at 50oC and was stable up to 70oC, retaining 93% of its initial activity after treatment for 1 hr. Furthermore, Ca 2+ ions (10 mM) significantly enhanced the thermal stability of the CGTase. The purified enzyme was active and stable over a wide pH range, showing maximal activity at pH 9.5. The enzyme was significantly stimulated by Zn 2+ , Ca 2+ and Co 2+ but was completely inhibited in the presence of Fe 3+ and mercaptoethanol. The K m and V max values of the purified CGTase were estimated to be 0.0434 mg/ml and 3,333.3 mg β-CD/ml/min, respectively. β-CD was the predominant product of starch degradation by the Amphibacillus sp. NRC-WN CGTase, followed by α-and γ-CDs. Conclusions: A new low molecular mass alkaline CGTase was purified from a newly identified alkaliphilic Amphibacillus sp. NRC-WN isolate from the Egyptian soda lakes. The enzyme showed promising thermal and pH stability and a high affinity toward starch as a natural substrate.

Properties of NAD (P) H Azoreductase from Alkaliphilic Red Bacteria Aquiflexum sp. DL6

Azoreductase plays a key role in bioremediation and biotransformation of azo dyes. It initializes the reduction of azo bond in azo dye metabolism under aerobic or anaerobic conditions. In the present study, we isolated an alkaliphilic red-colored Aquiflexum sp. DL6 bacterial strain and identified by 16S rRNA method. We report nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-dependent azoreductase purified from Aquiflexum sp. DL6 by a combination of ammonium sulfate precipitation and chromatography methods. The azoreductase was purified up to 30-fold with 37% recovery. The molecular weight was found to be 80kDa. The optimum activity was observed at pH 7.4 and temperature 60°C with amaranth azo dye as a substrate. The thermal stability of azoreductase was up to 80°C. The azoreductase has shown a wide range of substrate specificity, including azo dyes and nitro aromatic compounds. Metal ions have no significant inhibitory action on azoreductase activity. The apparent K m and V max values for amaranth azo dye were 1.11mM and 30.77U/mg protein respectively. This NAD (P) H azoreductase represents the first azoreductase to be characterized from alkaliphilic bacteria.

PGIAK1, a Heavy Metal Resistant Plasmid from an Obligate Alkaliphilic and Halotolerant Bacterium Isolated from the Antarctic Concordia Station Confined Environment

pGIAK1 is a 38-kb plasmid originating from the obligate alkaliphilic and halotolerant Bacillaceae strain JMAK1. The strain was originally isolated from the confined environments of the Antarctic Concordia station. Analysis of the pGIAK1 38,362-bp sequence revealed that, in addition to its replication region, this plasmid contains the genetic determinants for cadmium and arsenic resistances, putative methyltransferase, tyrosine recombinase, spore coat protein and potassium transport protein, as well as several hypothetical proteins. Cloning the pGIAK1 cad operon in Bacillus cereus H3081.97 and its ars operon in Bacillus subtilis 1A280 conferred to these hosts cadmium and arsenic resistances, respectively, therefore confirming their bona fide activities. The pGIAK1 replicon region was also shown to be functional in Bacillus thuringiensis, Bacillus subtilis and Staphylococcus aureus, but was only stably maintained in B. subtilis. Finally, using an Escherichia coli - B. thuringiensis shuttle BAC vector, pGIAK1 was shown to display conjugative properties since it was able to transfer the BAC plasmid among B. thuringiensis strains.

Effect of unconventional carbon sources on biosurfactant production and its application in bioremediation

The potential of an alkaliphilic bacterium Klebsiella sp. strain RJ-03, to utilize different unconventional carbon sources for the production of biosurfactant was evaluated. The biosurfactant produced using corn powder, potato peel powder, Madhuca indica and sugarcane bagasse containing medium, exhibited significantly higher viscosity and maximum reduction in surface tension as compared to other substrates. Among several carbon substrates tested, production of biosurfactant was found to be the highest with corn powder (15.40±0.21g/l) as compared to others. The comparative chemical characterization of purified biosurfactant was done using advance analytical tools such as NMR, FT-IR, SEM, GPC, MALDI TOF–TOF MS, GC–MS, TG and DSC. Analyses indicated variation in the functional groups, monosaccharide composition, molecular mass, thermostability. Higher yield with cheaper raw materials, noteworthy stress tolerance of CP-biosurfactant toward pH and salt as well as compatibility with chemical surfactants and detergents revealed its potential for commercialization and application in bioremediation.

English

We partially purified extracellular metalloprotease of a halotolerant alkaliphilic bacterium isolated from coastal sediment of Goa, India, which was identified as Bacillus cereus strain CS1 based on biochemical characteristics and 16S rDNA sequence. Zymogram of partially purified enzyme clearly revealed two prominent protease isozymes of 210 and 215 kDa. Although, protease showed activity over a wide range of pH (pH 8 to 12) and temperature (30, 37, 45 and 50°C), optimum pH and temperature were 9 and 37°C, respectively. Protease exhibited extreme halotolerance upto 8% NaCl making it one of the industrially valuable enzyme. Among different carbon sources, glucose (1%) enhanced maximum enzyme activity (71U/ml), whereas, among the nitrogen sources, tryptone (0.2%) proved best to enhance enzyme activity (158U/ml). Ca++ ions enhanced protease activity by 7%, whereas, Cu ++ , Mg ++ , Pb ++ and Hg ++ ions inhibited activity by 91, 79, 87 and 77%, respectively. Among inhibitors tested, protease activity was significantly inhibited by Na2–EDTA as residual enzyme activity was only 21%, which clearly confirmed it to be a metalloprotease. The partially purified protease mixed separately with two detergents Rin and Wheel clearly demonstrated significant stain removing capability. Thus, protease produced by Bacillus is a potential candidate as an additive in detergent industry. Keywords: Halo-tolerant, isozymes, zymogram, metalloprotease. African Journal of Biotechnology Vol. 12(31), pp. 4905-4914

Draft Genome Sequence of Amphibacillus jilinensis Y1T, a Facultatively Anaerobic, Alkaliphilic and Halotolerant Bacterium

The genus Amphibacillus was established in 1990, and seven additional species were described in the past two decades. Amphibacillus jilinensis Y1T is a facultatively anaerobic and alkaliphilic bacterium isolated from a soda lake in China. Here we describe the structural and genetic features of the draft genome about the type strain Y1T (3,831,075 bp, with a G+C content of 37.27%). This is the first genome report of the Amphibacillus genus.