bfr protein (Rhodopseudomonas palustris CGA009)

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

bfr

Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (160 aa)

Predicted Functional Partners:

hemZ

0.921

pigA

0.904

RPA1539

0.901

RPA0359

0.900

cycA-2

0.741

RPA2434

0.733

RPA1246

0.642

RPA1500

0.642

katE

0.569

puhA

0.551

Your Current Organism:

Rhodopseudomonas palustris CGA009

NCBI taxonomy Id: 258594
Other names: R. palustris CGA009, Rhodopseudomonas palustris str. CGA009, Rhodopseudomonas palustris strain CGA009

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
RPA0359	RPA1539	RPA0359	RPA1539	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Bacteriophytochrome, apparent pseudogene, frameshifted; High identity to bacteriophytochrome from a photosynthetic Bradyrhizobium (strain ORS278) that controls photosystem synthesis; Citation: Giraud E, Fardoux J, Fourrier N, Hannibal L, Genty B, Bouyer P, Dreyfus B, Vermeglio A. Bacteriophytochrome controls photosystem synthesis in anoxygenic bacteria. Nature. 2002 May 9;417(6885):202-5.	0.917
RPA0359	bfr	RPA0359	RPA3600	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.900
RPA0359	hemZ	RPA0359	RPA0875	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.	0.908
RPA0359	pigA	RPA0359	RPA3279	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Possible iron-starvation protein.	0.900
RPA1246	bfr	RPA1246	RPA3600	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.642
RPA1246	katE	RPA1246	RPA3310	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.	0.447
RPA1500	bfr	RPA1500	RPA3600	Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.642
RPA1500	katE	RPA1500	RPA3310	Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.	0.447
RPA1539	RPA0359	RPA1539	RPA0359	Bacteriophytochrome, apparent pseudogene, frameshifted; High identity to bacteriophytochrome from a photosynthetic Bradyrhizobium (strain ORS278) that controls photosystem synthesis; Citation: Giraud E, Fardoux J, Fourrier N, Hannibal L, Genty B, Bouyer P, Dreyfus B, Vermeglio A. Bacteriophytochrome controls photosystem synthesis in anoxygenic bacteria. Nature. 2002 May 9;417(6885):202-5.	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	0.917
RPA1539	bfr	RPA1539	RPA3600	Bacteriophytochrome, apparent pseudogene, frameshifted; High identity to bacteriophytochrome from a photosynthetic Bradyrhizobium (strain ORS278) that controls photosystem synthesis; Citation: Giraud E, Fardoux J, Fourrier N, Hannibal L, Genty B, Bouyer P, Dreyfus B, Vermeglio A. Bacteriophytochrome controls photosystem synthesis in anoxygenic bacteria. Nature. 2002 May 9;417(6885):202-5.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.901
RPA1539	hemZ	RPA1539	RPA0875	Bacteriophytochrome, apparent pseudogene, frameshifted; High identity to bacteriophytochrome from a photosynthetic Bradyrhizobium (strain ORS278) that controls photosystem synthesis; Citation: Giraud E, Fardoux J, Fourrier N, Hannibal L, Genty B, Bouyer P, Dreyfus B, Vermeglio A. Bacteriophytochrome controls photosystem synthesis in anoxygenic bacteria. Nature. 2002 May 9;417(6885):202-5.	Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.	0.923
RPA1539	pigA	RPA1539	RPA3279	Bacteriophytochrome, apparent pseudogene, frameshifted; High identity to bacteriophytochrome from a photosynthetic Bradyrhizobium (strain ORS278) that controls photosystem synthesis; Citation: Giraud E, Fardoux J, Fourrier N, Hannibal L, Genty B, Bouyer P, Dreyfus B, Vermeglio A. Bacteriophytochrome controls photosystem synthesis in anoxygenic bacteria. Nature. 2002 May 9;417(6885):202-5.	Possible iron-starvation protein.	0.900
RPA2434	bfr	RPA2434	RPA3600	Sensor histidine kinase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.733
bfr	RPA0359	RPA3600	RPA0359	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	0.900
bfr	RPA1246	RPA3600	RPA1246	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Conserved unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	0.642
bfr	RPA1500	RPA3600	RPA1500	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	0.642
bfr	RPA1539	RPA3600	RPA1539	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Bacteriophytochrome, apparent pseudogene, frameshifted; High identity to bacteriophytochrome from a photosynthetic Bradyrhizobium (strain ORS278) that controls photosystem synthesis; Citation: Giraud E, Fardoux J, Fourrier N, Hannibal L, Genty B, Bouyer P, Dreyfus B, Vermeglio A. Bacteriophytochrome controls photosystem synthesis in anoxygenic bacteria. Nature. 2002 May 9;417(6885):202-5.	0.901
bfr	RPA2434	RPA3600	RPA2434	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Sensor histidine kinase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.	0.733
bfr	cycA-2	RPA3600	RPA2314	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Cytochrome c556; Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.	0.741
bfr	hemZ	RPA3600	RPA0875	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.	0.921

page 1 of 2

Server load: medium (58%) [HD]

Permalink

Network

Neighborhood

Databases

Co-occurrence

Textmining

Co-expression

Experiments

Fusion

© STRING Consortium 2026

Credits

Access

Info

About