ywrO protein (Streptomyces turgidiscabies) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

Node Color

colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Knowledge-based Evidence

from curated databases

textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Input:

Neighborhood

Gene Fusion

Co-occurrence

Co-expression

Experiments

Databases

Textmining

[Homology]

Score

ywrO

General stress protein 14. (180 aa)

Predicted Functional Partners:

ubiE_7

0.715

yhaU

0.581

nhaS3_1

0.581

nhaS3_2

0.581

nuoB

0.553

nqo6

0.553

T45_04502

0.551

yhdN_6

0.548

azoB_2

0.539

qorB_1

0.530

Your Current Organism:

Streptomyces turgidiscabies

NCBI taxonomy Id: 85558
Other names: ATCC 700248, CIP 105577, IFO 16080, JCM 10429, NBRC 16080, NRRL B-24078, S. turgidiscabies, strain SY9113

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc.

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
T45_04502	ywrO	T45_04502	T45_04503	Hypothetical protein.	General stress protein 14.	0.551
azoB_2	nqo6	T45_08609	T45_07255	NAD(P)H azoreductase.	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	0.824
azoB_2	nuoB	T45_08609	T45_07217	NAD(P)H azoreductase.	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	0.824
azoB_2	ubiE_7	T45_08609	T45_07262	NAD(P)H azoreductase.	Ubiquinone/menaquinone biosynthesis methyltransferase; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).	0.534
azoB_2	ywrO	T45_08609	T45_04503	NAD(P)H azoreductase.	General stress protein 14.	0.539
nhaS3_1	ywrO	T45_05472	T45_04503	High-affinity Na(+)/ H(+) antiporter NhaS3.	General stress protein 14.	0.581
nhaS3_2	ywrO	T45_06232	T45_04503	High-affinity Na(+)/ H(+) antiporter NhaS3.	General stress protein 14.	0.581
nqo6	azoB_2	T45_07255	T45_08609	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	NAD(P)H azoreductase.	0.824
nqo6	nuoB	T45_07255	T45_07217	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	0.933
nqo6	qorB_1	T45_07255	T45_02226	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	Quinone oxidoreductase 2.	0.824
nqo6	ywrO	T45_07255	T45_04503	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	General stress protein 14.	0.553
nuoB	azoB_2	T45_07217	T45_08609	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	NAD(P)H azoreductase.	0.824
nuoB	nqo6	T45_07217	T45_07255	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	0.933
nuoB	qorB_1	T45_07217	T45_02226	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	Quinone oxidoreductase 2.	0.824
nuoB	ywrO	T45_07217	T45_04503	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	General stress protein 14.	0.553
qorB_1	nqo6	T45_02226	T45_07255	Quinone oxidoreductase 2.	NADH-quinone oxidoreductase subunit 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	0.824
qorB_1	nuoB	T45_02226	T45_07217	Quinone oxidoreductase 2.	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.	0.824
qorB_1	ubiE_7	T45_02226	T45_07262	Quinone oxidoreductase 2.	Ubiquinone/menaquinone biosynthesis methyltransferase; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).	0.838
qorB_1	ywrO	T45_02226	T45_04503	Quinone oxidoreductase 2.	General stress protein 14.	0.530
ubiE_7	azoB_2	T45_07262	T45_08609	Ubiquinone/menaquinone biosynthesis methyltransferase; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).	NAD(P)H azoreductase.	0.534