groS protein (Croceitalea dokdonensis) - STRING interaction network

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Score

groS

Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (92 aa)

Predicted Functional Partners:

groL

0.999

dnaK

0.970

grpE

0.945

I595_2253

0.866

rplL

0.733

clpP-2

0.721

clpP

0.716

dnaJ

0.707

clpB

0.700

I595_1584

0.680

Your Current Organism:

Croceitalea dokdonensis

NCBI taxonomy Id: 1300341
Other names: C. dokdonensis DOKDO 023, Croceitalea dokdonensis DOKDO 023

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
I595_1584	I595_2253	I595_1584	I595_2253	Heat shock protein DnaJ-like protein.	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	0.974
I595_1584	clpB	I595_1584	I595_556	Heat shock protein DnaJ-like protein.	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	0.795
I595_1584	clpP	I595_1584	I595_2376	Heat shock protein DnaJ-like protein.	ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	0.500
I595_1584	clpP-2	I595_1584	I595_887	Heat shock protein DnaJ-like protein.	ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	0.500
I595_1584	dnaK	I595_1584	I595_524	Heat shock protein DnaJ-like protein.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.994
I595_1584	groL	I595_1584	I595_1062	Heat shock protein DnaJ-like protein.	Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.827
I595_1584	groS	I595_1584	I595_1061	Heat shock protein DnaJ-like protein.	Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.680
I595_1584	grpE	I595_1584	I595_3242	Heat shock protein DnaJ-like protein.	Molecular chaperone GrpE; 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 [...]	0.923
I595_2253	I595_1584	I595_2253	I595_1584	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Heat shock protein DnaJ-like protein.	0.974
I595_2253	clpB	I595_2253	I595_556	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	0.743
I595_2253	dnaJ	I595_2253	I595_3243	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Chaperone 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, D [...]	0.971
I595_2253	dnaK	I595_2253	I595_524	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.999
I595_2253	groL	I595_2253	I595_1062	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.942
I595_2253	groS	I595_2253	I595_1061	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.866
I595_2253	grpE	I595_2253	I595_3242	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	Molecular chaperone GrpE; 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 [...]	0.777
clpB	I595_1584	I595_556	I595_1584	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	Heat shock protein DnaJ-like protein.	0.795
clpB	I595_2253	I595_556	I595_2253	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	Heat shock protein 90; Molecular chaperone. Has ATPase activity.	0.743
clpB	clpP	I595_556	I595_2376	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	0.875
clpB	clpP-2	I595_556	I595_887	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	0.874
clpB	dnaJ	I595_556	I595_3243	Putative heat shock ClpB protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.	Chaperone 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, D [...]	0.786