Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Streptomyces sp. A108 isolate:Streptomyces sp.

ABSTRACT: Streptomyces sp. A108 isolate:Streptomyces sp. Genome sequencing and assembly

PROVIDER: PRJNA644752 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

Streptomyces sp. M7 LC-MS - Streptomyces sp. M7 has demonstrated ability to remove lindane from culture media and soils

Project description:Streptomyces sp. M7 has demonstrated ability to remove lindane from culture media and soils. In this study, we used MS-based label-free quantitative proteomic to understand lindane degradation and its metabolic context in Streptomyces sp. M7. We identified the proteins involved in the up-stream degradation pathway. Our results demonstrated that mineralization of lindane is feasible since proteins from an unusual down-stream degradation pathway were also identified. Degradative steps were supported by an active catabolism that supplied energy and reducing equivalents in the form of NADPH. This is the first study in which degradation steps of an organochlorine compound and metabolic context are elucidate in a biotechnological genus as Streptomyces. These results serve as basement to study other degradative actinobacteria and to improve the degradation processes of Streptomyces sp. M7.

2018-08-10 | PXD010607 | Pride

Total protein of S. aureus treated and untreated with Streptomyces sp. GKU 223

Project description:This study is aimed to isolate marine actinomycetes from sediments from Andaman and the Gulf of Thailand. All 101 marine actinomycetes were screened for anti-biofilm activity. Streptomyces sp. GKU223 showed significantly inhibited biofilm formation of S. aureus. The evaluation of supernatants of anti-biofilm activity produced by Streptomyces sp. GKU223 has been performed. Since the interaction between marine actinomycetes and biofilm forming bacteria has never been investigated, proteomic analysis has been used to identify whole cell proteins involved in anti–biofilm activity. Understanding the interaction at molecular level will lead to sustainably use for anti-biofilm producing marine actinomycetes in pharmaceutical and medicinal applications in the future.

2018-08-20 | PXD010815 | JPOST Repository

Analysis of Escherichia coli treated and untreated with Streptomyces sp. GKU 257-1

Project description:This study is aimed to isolate marine actinomycetes from sediments from Andaman and the Gulf of Thailand. All 101 marine actinomycetes were screened for anti-biofilm activity. Streptomyces sp. GKU 257-1 showed significantly inhibited biofilm formation of E. coli. The evaluation of supernatants of anti-biofilm activity produced by Streptomyces sp. GKU 257-1 has been performed. Since the interaction between marine actinomycetes and biofilm forming bacteria has never been investigated, proteomic analysis has been used to identify whole cell proteins involved in anti–biofilm activity. Understanding the interaction at molecular level will lead to sustainably use for anti-biofilm producing marine actinomycetes in pharmaceutical and medicinal applications in the future.

2019-09-07 | PXD011027 | JPOST Repository

Examination of polyester-polyurethane degradation by Streptomyces sp. PU10

Project description:This study aimed to investigate the variations in the protein composition of Streptomyces sp. PU10 when cultivated with either Impranil (polyestere-polyurethane) or glucose as the carbon source. We analyzed both the intracellular and extracellular protein fractions to gain insights into the intricate processes involving PU degradation, intermediate metabolic pathways in PU degradation, and the connection between primary and secondary metabolism within Streptomyces sp. PU10.

2024-03-29 | PXD047534 | Pride

Proteomics analysis of streptomyces sp. MBT76 demonstrates the production of qinichelins, new mixed catecholate-hydroxamate siderophores

Project description:Actinomycete genomes contain a plethora of orphan gene clusters encoding unknown secondary metabolites, and representing a huge unexploited pool of chemical diversity. The explosive increase in genome sequencing and the massive advance of bioinformatic tools have revolutionized the rationale for natural product discovery from actinomycetes. In this context, we applied a genome mining approach to discover a group of unique catecholate-hydroxamate siderophores termed as qinichelins from Streptomyces sp. MBT76. Quantitative proteomics statistically correlated a gene cluster of interest (qch) to its unknown chemotype (qinichelin), after which structural elucidation of isolated qinichelin was assisted by bioinformatics analysis and verified by MS2 and NMR experiments. Strikingly, intertwined functional crosstalk among four separately located gene clusters was implicated in the biosynthesis of qinichelins.

2018-10-24 | PXD006577 | Pride

Streptomyces sp. PLM4 isolate:PLM4

Project description:Streptomyces sp. PLM4 isolate:PLM4 Genome sequencing and assembly

| PRJNA820554 | ENA

Streptomyces sp. FXP04 isolate:FXP04

Project description:Streptomyces sp. FXP04 isolate:FXP04 Genome sequencing and assembly

| PRJNA756417 | ENA

Streptomyces sp. NBC00162 isolate:NBC00162

Project description:Streptomyces sp. NBC00162 isolate:NBC00162 Genome sequencing and assembly

| PRJNA689727 | ENA

Streptomyces sp. MB42 proteomics response to catechin, dopamine, phenylephrine

Project description:Streptomyces sp. MB42 produces antimicrobial compound under the pressence of specific compounds. This experiment is to see which gene cluster upregulated during the treatment of target compound.

2022-02-04 | PXD029669 | Pride

Proteogenomic of Blastocystis sp. subtype 4 isolate WR1

Project description:description Blastocystis sp. is a highly prevalent anaerobic eukaryotic parasite of humans and animals. The genome of several representatives has been sequenced revealing specific traits such as an intriguing 3’-end processing of primary transcripts. We have acquired a first high-throughput proteomics dataset on the difficult to cultivate ST4 isolate WR1 and detected 2,761 proteins. We evidenced for the first time by proteogenomics a functional termination codon derived from transcript polyadenylation for seven different key cellular components.

2017-09-11 | PXD006588 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data