(12 nodes) Stress response, and Protein folding chaperone network (Dechloromonas aromatica)

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Your Input:
	hslV	HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (178 aa)
	hslU	Heat shock protein 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. (446 aa)
	groS	Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
	groL	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (550 aa)
	dnaJ	Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] (378 aa)
	dnaK	Heat shock protein Hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. (645 aa)
	grpE	GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] (184 aa)
	htpG	Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. (636 aa)
	Daro_2058	Heat shock protein DnaJ, N-terminal. (108 aa)
	dnaJ-2	DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] (335 aa)
	Daro_3428	Molecular chaperone-like protein. (148 aa)
	Daro_3636	Heat shock protein DnaJ, N-terminal. (92 aa)

Your Current Organism:

Dechloromonas aromatica

NCBI taxonomy Id: 159087
Other names: D. aromatica RCB, Dechloromonas aromatica RCB, Dechloromonas aromatica str. RCB, Dechloromonas sp. RCB

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Daro_2058	Daro_3428	Daro_2058	Daro_3428	Heat shock protein DnaJ, N-terminal.	Molecular chaperone-like protein.	0.926
Daro_2058	Daro_3636	Daro_2058	Daro_3636	Heat shock protein DnaJ, N-terminal.	Heat shock protein DnaJ, N-terminal.	0.772
Daro_2058	dnaJ-2	Daro_2058	Daro_2467	Heat shock protein DnaJ, N-terminal.	DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...]	0.769
Daro_2058	dnaK	Daro_2058	Daro_0923	Heat shock protein DnaJ, N-terminal.	Heat shock protein Hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.925
Daro_2058	groL	Daro_2058	Daro_0426	Heat shock protein DnaJ, N-terminal.	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.746
Daro_2058	groS	Daro_2058	Daro_0425	Heat shock protein DnaJ, N-terminal.	Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.557
Daro_2058	grpE	Daro_2058	Daro_0924	Heat shock protein DnaJ, N-terminal.	GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]	0.869
Daro_2058	hslU	Daro_2058	Daro_0204	Heat shock protein DnaJ, N-terminal.	Heat shock protein 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.	0.512
Daro_2058	hslV	Daro_2058	Daro_0203	Heat shock protein DnaJ, N-terminal.	HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.426
Daro_2058	htpG	Daro_2058	Daro_1127	Heat shock protein DnaJ, N-terminal.	Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity.	0.728
Daro_3428	Daro_2058	Daro_3428	Daro_2058	Molecular chaperone-like protein.	Heat shock protein DnaJ, N-terminal.	0.926
Daro_3428	Daro_3636	Daro_3428	Daro_3636	Molecular chaperone-like protein.	Heat shock protein DnaJ, N-terminal.	0.947
Daro_3428	dnaJ	Daro_3428	Daro_0922	Molecular chaperone-like protein.	Heat shock protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	0.950
Daro_3428	dnaJ-2	Daro_3428	Daro_2467	Molecular chaperone-like protein.	DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...]	0.950
Daro_3428	groL	Daro_3428	Daro_0426	Molecular chaperone-like protein.	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.923
Daro_3428	groS	Daro_3428	Daro_0425	Molecular chaperone-like protein.	Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.848
Daro_3428	grpE	Daro_3428	Daro_0924	Molecular chaperone-like protein.	GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]	0.987
Daro_3428	hslU	Daro_3428	Daro_0204	Molecular chaperone-like protein.	Heat shock protein 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.	0.619
Daro_3428	hslV	Daro_3428	Daro_0203	Molecular chaperone-like protein.	HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.592
Daro_3428	htpG	Daro_3428	Daro_1127	Molecular chaperone-like protein.	Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity.	0.952