trxA_2 protein (Legionella cherrii) - STRING interaction network

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Score

trxA_2

Thioredoxin; Belongs to the thioredoxin family. (108 aa)

Predicted Functional Partners:

trxB

0.972

rho

0.649

fur

0.578

rsmE

0.562

htpB

0.556

gor

0.537

hslV

0.536

hslU

0.525

rir1

0.519

msrA_1

0.498

Your Current Organism:

Legionella cherrii

NCBI taxonomy Id: 28084
Other names: ATCC 35252, CCUG 29666, CIP 103842, DSM 19213, L. cherrii, Legionella cherryi, NCTC 11976, strain ORW

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
fur	trxA_2	Lche_3330	Lche_2849	Ferric uptake regulation protein; Belongs to the Fur family.	Thioredoxin; Belongs to the thioredoxin family.	0.578
gor	msrA_1	Lche_2527	Lche_2831	Glutathione reductase.	Bifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	0.602
gor	trxA_2	Lche_2527	Lche_2849	Glutathione reductase.	Thioredoxin; Belongs to the thioredoxin family.	0.537
gor	trxB	Lche_2527	Lche_1364	Glutathione reductase.	Thioredoxin reductase.	0.469
hslU	hslV	Lche_2470	Lche_2471	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	Peptidase component of the HslUV protease (Heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.999
hslU	htpB	Lche_2470	Lche_0201	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.919
hslU	trxA_2	Lche_2470	Lche_2849	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	Thioredoxin; Belongs to the thioredoxin family.	0.525
hslV	hslU	Lche_2471	Lche_2470	Peptidase component of the HslUV protease (Heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	0.999
hslV	htpB	Lche_2471	Lche_0201	Peptidase component of the HslUV protease (Heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.842
hslV	trxA_2	Lche_2471	Lche_2849	Peptidase component of the HslUV protease (Heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	Thioredoxin; Belongs to the thioredoxin family.	0.536
htpB	hslU	Lche_0201	Lche_2470	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	0.919
htpB	hslV	Lche_0201	Lche_2471	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Peptidase component of the HslUV protease (Heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.842
htpB	msrA_1	Lche_0201	Lche_2831	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Bifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	0.495
htpB	rir1	Lche_0201	Lche_1805	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.	0.473
htpB	trxA_2	Lche_0201	Lche_2849	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Thioredoxin; Belongs to the thioredoxin family.	0.556
msrA_1	gor	Lche_2831	Lche_2527	Bifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	Glutathione reductase.	0.602
msrA_1	htpB	Lche_2831	Lche_0201	Bifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.495
msrA_1	trxA_2	Lche_2831	Lche_2849	Bifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	Thioredoxin; Belongs to the thioredoxin family.	0.498
msrA_1	trxB	Lche_2831	Lche_1364	Bifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.	Thioredoxin reductase.	0.506
rho	rir1	Lche_2848	Lche_1805	Hypothetical protein; Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA- dependent ATPase activity, and release of the mRNA from the DNA template.	Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.	0.404