groS protein (Synechococcus sp. CC9605) - STRING interaction network

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groS

Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (103 aa)

Predicted Functional Partners:

groL2

0.997

groL1

0.993

grpE

0.978

ABB35158.1

0.912

dnaK

0.890

dnaK-2

0.885

ABB35899.1

0.824

rplL

0.754

dnaJ

0.716

hrcA

0.707

Your Current Organism:

Synechococcus sp. CC9605

NCBI taxonomy Id: 110662
Other names: S. sp. CC9605

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ABB35158.1	ABB35899.1	Syncc9605_1404	Syncc9605_2160	ATP-binding region, ATPase-like.	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	0.951
ABB35158.1	dnaJ	Syncc9605_1404	Syncc9605_0024	ATP-binding region, ATPase-like.	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, [...]	0.863
ABB35158.1	dnaK	Syncc9605_1404	Syncc9605_1396	ATP-binding region, ATPase-like.	Molecular chaperone DnaK, heat shock protein HSP70; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.973
ABB35158.1	dnaK-2	Syncc9605_1404	Syncc9605_2674	ATP-binding region, ATPase-like.	Heat shock protein Hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.970
ABB35158.1	groL1	Syncc9605_1404	Syncc9605_0615	ATP-binding region, ATPase-like.	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.797
ABB35158.1	groL2	Syncc9605_1404	Syncc9605_2169	ATP-binding region, ATPase-like.	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.835
ABB35158.1	groS	Syncc9605_1404	Syncc9605_2170	ATP-binding region, ATPase-like.	Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.912
ABB35158.1	grpE	Syncc9605_1404	Syncc9605_0023	ATP-binding region, ATPase-like.	Putative heat shock protein 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 round [...]	0.798
ABB35899.1	ABB35158.1	Syncc9605_2160	Syncc9605_1404	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	ATP-binding region, ATPase-like.	0.951
ABB35899.1	dnaJ	Syncc9605_2160	Syncc9605_0024	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	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, [...]	0.886
ABB35899.1	groL1	Syncc9605_2160	Syncc9605_0615	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.781
ABB35899.1	groL2	Syncc9605_2160	Syncc9605_2169	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.781
ABB35899.1	groS	Syncc9605_2160	Syncc9605_2170	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.824
ABB35899.1	grpE	Syncc9605_2160	Syncc9605_0023	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	Putative heat shock protein 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 round [...]	0.917
ABB35899.1	hrcA	Syncc9605_2160	Syncc9605_2417	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.	0.699
dnaJ	ABB35158.1	Syncc9605_0024	Syncc9605_1404	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, [...]	ATP-binding region, ATPase-like.	0.863
dnaJ	ABB35899.1	Syncc9605_0024	Syncc9605_2160	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, [...]	Putative DnaK-type molecular chaperone (HSP70 family); Belongs to the heat shock protein 70 family.	0.886
dnaJ	dnaK	Syncc9605_0024	Syncc9605_1396	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, [...]	Molecular chaperone DnaK, heat shock protein HSP70; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.943
dnaJ	dnaK-2	Syncc9605_0024	Syncc9605_2674	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, [...]	Heat shock protein Hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.943
dnaJ	groL1	Syncc9605_0024	Syncc9605_0615	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, [...]	Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.530