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Saccharomonospora viridis

ABSTRACT: Pneumonia causing bacterium

PROVIDER: PRJNA60967 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
		Other
	JRZE01.dat.gz	Other
	JRZE01.fasta.gz	Fasta.gz
	JRZE01.master.dat	Other
	DRR100117_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Saccharomonospora viridis

Project description:Pneumonia causing bacterium

| PRJNA60967 | ENA

Complete genome sequence of Saccharomonospora viridis type strain (P101).

Project description:Saccharomonospora viridis (Schuurmans et al. 1956) Nonomurea and Ohara 1971 is the type species of the genus Saccharomonospora which belongs to the family Pseudonocardiaceae. S. viridis is of interest because it is a Gram-negative organism classified among the usually Gram-positive actinomycetes. Members of the species are frequently found in hot compost and hay, and its spores can cause farmer's lung disease, bagassosis, and humidifier fever. Strains of the species S. viridis have been found to metabolize the xenobiotic pentachlorophenol (PCP). The strain described in this study has been isolated from peat-bog in Ireland. Here we describe the features of this organism, together with the complete genome sequence, and annotation. This is the first complete genome sequence of the family Pseudonocardiaceae, and the 4,308,349 bp long single replicon genome with its 3906 protein-coding and 64 RNA genes is part of the Genomic Encyclopedia of Bacteria and Archaea project.

| S-EPMC3035233 | biostudies-literature

Nematicidal activity of thermostable alkaline protease produced by Saccharomonospora viridis strain Hw G550.

Project description:Application of thermostable alkaline protease to control the harmful nematodes was investigated in the current study. A total of 14 proteolytic actinomycetes were isolated from Egyptian harsh environments. Out of them, isolate G550 exhibited the highest proteolytic activity (528.9 U/ml). Protease from isolate G550 exhibited high nematicidal activity against M. incognita under laboratory conditions and caused hydrolysis of J2S cuticle. This isolate was identified using molecular techniques and deposited in GenBank under name of Saccharomonospora viridis strain Hw G550 with accession number: MF152631. The G550 protease was extracted, characterized and applied under greenhouse conditions as nematicidal agent. This enzyme exhibited maximum activity and stability at alkaline pH (8) and thermal conditions (50-60?°C). Also, the results showed that, all treatments using protease caused a significant decrease in nematode reproduction and increasing in the plant properties. Finally, the thermo alkaliphilic protease could be used as bio-control agent against RKN.

| S-EPMC6864322 | biostudies-literature

Saccharomonospora xinjiangensis

Project description:Soil bacterium

| PRJNA62253 | ENA

Saccharomonospora saliphila

Project description:Halophilic soil bacterium

| PRJNA66585 | ENA

Saccharomonospora viridis DSM 43017

Project description:Causes hypersensitivity pneumonitis

| PRJNA20835 | ENA

Application of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp.

Project description:Saccharomonospora viridis is a thermophilic actinomycete that may have biotechnological applications because of its dye decolorizing activity, though the enzymatic oxidative system responsible for this activity remains elusive. Bioinformatic analysis revealed a DyP-type peroxidase gene in the genome of S. viridis DSM 43017 with sequence similarity to peroxidase from dye-decolorizing microbes. This gene, svidyp, consists of 1,215 bp encoding a polypeptide of 404 amino acids. The gene encoding SviDyP was cloned, heterologously expressed in Escherichia coli, and then purified. The recombinant protein could efficiently decolorize several triarylmethane dyes, anthraquinonic and azo dyes under neutral to alkaline conditions. The optimum pH and temperature for SviDyP was pH 7.0 and 70°C, respectively. Compared with other DyP-type peroxidases, SviDyP was more active at high temperatures, retaining>63% of its maximum activity at 50-80°C. It also showed broad pH adaptability (>35% activity at pH 4.0-9.0) and alkali-tolerance (>80% activity after incubation at pH 5-10 for 1 h at 37°C), and was highly thermostable (>60% activity after incubation at 70°C for 2 h at pH 7.0). SviDyP had an accelerated action during the biobleaching of eucalyptus kraft pulp, resulting in a 21.8% reduction in kappa number and an increase of 2.98% (ISO) in brightness. These favorable properties make SviDyP peroxidase a promising enzyme for use in the pulp and paper industries.

| S-EPMC4204856 | biostudies-literature

Inhibition of Staphylococcus aureus biofilm formation by gurmarin, a plant-derived cyclic peptide

Project description:Staphylococcus aureus is an opportunistic pathogen capable of causing various infections ranging from superficial skin infections to life-threatening severe diseases, including pneumonia and sepsis. This bacterium is attached to biotic and abiotic surfaces and forms biofilms that are resistant to conventional antimicrobial agents and clearance by host defenses. Infections associated with biofilms may result in longer hospitalizations, a need for surgery, and may even result in death. Agents that inhibit the formation of biofilms and virulence without affecting bacterial growth to avoid the development of drug resistance could be useful for therapeutic purposes. In this regard, we identified and isolated a small cyclic peptide, gurmarin, from a plant source that inhibited the formation of S. aureus biofilm without affecting the growth rate of the bacterium. We determined the gene expression of S. aureus biofilm treated with gurmarin and compared it to the untreated control biofilms. Differentially expressed genes were identified and their roles in the inhibition of S. aureus biofilms by gurmarin were analyzed.

2022-09-21 | E-MTAB-12154 | biostudies-arrayexpress

Saccharomonospora iraqiensis subsp. paurometabolica

Project description:Halophilic bacterium

| PRJNA61913 | ENA

The small regulatory RNA Lpr10 regulates the expression of RpoS in Legionella pneumophila

Project description:Legionella pneumophila (Lp) is a waterborne bacterium able to infect human alveolar macrophages, causing a severe pneumonia known as Legionnaires’ disease. In water, Lp grows inside ciliates and ameoba. Lp is able to survive for several months in water, while searching for host cells. In Lp, the sigma factor RpoS is important for survival in water. Several small regulatory RNAs (sRNA) are known to regulate the expression of RpoS in other bacteria. A previous transcriptomic study showed that RpoS positively regulates the sRNA Lpr10 in Lp. Microarray analysis was performed to investigate the genes regulated by Lpr10.

2020-05-27 | GSE151162 | GEO

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