Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Providencia stuartii

ABSTRACT: Normal gastrointestinal bacterium

PROVIDER: PRJNA34973 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other
	DRR015744_1.fastq.gz	Fastqsanger.gz
	DRR015744_2.fastq.gz	Fastqsanger.gz
	DRR015745_1.fastq.gz	Fastqsanger.gz
	DRR015745_2.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 631

Similar Datasets

Complete genome sequence of Providencia stuartii clinical isolate MRSN 2154.

Project description:Here we present the complete genome sequence of Providencia stuartii MRSN 2154, isolated from an Afghan national. P. stuartii is a Gram-negative bacillus capable of causing infections in a wide variety of human tissues. Because Providencia readily acquires plasmids bearing drug resistance loci, it is of growing clinical significance.

| S-EPMC3393513 | biostudies-literature

Full-Genome Assembly of Reference Strain Providencia stuartii ATCC 33672.

Project description:A member of the normal human gut microflora, Providencia stuartii is of clinical interest due to its role in nosocomial infections of the urinary tract and because it readily acquires antibiotic resistance. Here, we present the complete genome of P. stuartii strain ATCC 33672, consisting of a 4.28-Mbp chromosome and a 48.9-kbp plasmid.

| S-EPMC4208334 | biostudies-literature

Understanding Voltage Gating of Providencia stuartii Porins at Atomic Level.

Project description:Bacterial porins are water-filled β-barrel channels that allow translocation of solutes across the outer membrane. They feature a constriction zone, contributed by the plunging of extracellular loop 3 (L3) into the channel lumen. Porins are generally in the open state, but undergo gating in response to external voltages. To date the underlying mechanism is unclear. Here we report results from molecular dynamics simulations on the two porins of Providenica stuartii, Omp-Pst1 and Omp-Pst2, which display distinct voltage sensitivities. Voltage gating was observed in Omp-Pst2, where the binding of cations in-between L3 and the barrel wall results in exposing a conserved aromatic residue in the channel lumen, thereby halting ion permeation. Comparison of Omp-Pst1 and Omp-Pst2 structures and trajectories suggests that their sensitivity to voltage is encoded in the hydrogen-bonding network anchoring L3 onto the barrel wall, as we observed that it is the strength of this network that governs the probability of cations binding behind L3. That Omp-Pst2 gating is observed only when ions flow against the electrostatic potential gradient of the channel furthermore suggests a possible role for this porin in the regulation of charge distribution across the outer membrane and bacterial homeostasis.

| S-EPMC4425685 | biostudies-literature

Implication of porins in beta-lactam resistance of Providencia stuartii.

Project description:An integrative approach combining biophysical and microbiological methods was used to characterize the antibiotic translocation through the outer membrane of Providencia stuartii. Two novel members of the General Bacterial Porin family of Enterobacteriaceae, named OmpPst1 and OmpPst2, were identified in P. stuartii. In the presence of ertapenem (ERT), cefepime (FEP), and cefoxitin (FOX) in growth media, several resistant derivatives of P. stuartii ATCC 29914 showed OmpPst1-deficiency. These porin-deficient strains showed significant decrease of susceptibility to β-lactam antibiotics. OmpPst1 and OmpPst2 were purified to homogeneity and reconstituted into planar lipid bilayers to study their biophysical characteristics and their interactions with β-lactam molecules. Determination of β-lactam translocation through OmpPst1 and OmpPst2 indicated that the strength of interaction decreased in the order of ertapenem ≫ cefepime > cefoxitin. Moreover, the translocation of these antibiotics through OmpPst1 was more efficient than through OmpPst2. Heterologous expression of OmpPst1 in the porin-deficient E. coli strain BL21(DE3)omp8 was associated with a higher antibiotic susceptibility of the E. coli cells to β-lactams compared with expression of OmpPst2. All our data enlighten the involvement of porins in the resistance of P. stuartii to β-lactam antibiotics.

| S-EPMC2952228 | biostudies-literature

Providencia stuartii

Project description:WGS of NDM-producing Providencia thailandensis from Ukrainian patients

| PRJNA940352 | ENA

Providencia stuartii

Project description:Providencia stuartii Genome sequencing and assembly

| PRJNA848435 | ENA

Providencia stuartii

Project description:Whole genome sequencing of Providencia stuartii, an opportunistic pathogen

| PRJDB2801 | ENA

Providencia stuartii

Project description:Providencia stuartii