hslU protein (Wolinella succinogenes) - STRING interaction network

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Score

hslU

CLPY PROTEIN; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. (440 aa)

Predicted Functional Partners:

hslV

0.999

dnaJ

0.896

GRPE

0.893

GROEL

0.870

groS

0.862

htpG

0.862

lon

0.834

era

0.832

dnaK

0.811

WS1291

0.779

Your Current Organism:

Wolinella succinogenes

NCBI taxonomy Id: 273121
Other names: W. succinogenes DSM 1740, Wolinella succinogenes DSM 1740

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
GROEL	GRPE	WS0308	WS0495	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	0.979
GROEL	dnaJ	WS0308	WS0698	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN DNAJ PROTEIN; 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-dependen [...]	0.912
GROEL	dnaK	WS0308	WS0494	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	HEAT SHOCK PROTEIN, DNAK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.978
GROEL	groS	WS0308	WS0309	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	HEAT SHOCK PROTEIN GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.998
GROEL	hslU	WS0308	WS1293	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	CLPY PROTEIN; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.	0.870
GROEL	hslV	WS0308	WS1294	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	HEAT SHOCK PROTEIN; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.830
GROEL	htpG	WS0308	WS1737	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	CHAPERONE (HEAT SHOCK PROTEIN); Molecular chaperone. Has ATPase activity.	0.935
GROEL	lon	WS0308	WS1972	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	PUTATIVE ATP-DEPENDENT PROTEASE LA PROTEIN; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.	0.843
GRPE	GROEL	WS0495	WS0308	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.979
GRPE	dnaJ	WS0495	WS0698	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN DNAJ PROTEIN; 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-dependen [...]	0.975
GRPE	dnaK	WS0495	WS0494	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	HEAT SHOCK PROTEIN, DNAK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.998
GRPE	groS	WS0495	WS0309	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	HEAT SHOCK PROTEIN GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.921
GRPE	hslU	WS0495	WS1293	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	CLPY PROTEIN; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.	0.893
GRPE	hslV	WS0495	WS1294	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	HEAT SHOCK PROTEIN; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.874
GRPE	htpG	WS0495	WS1737	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	CHAPERONE (HEAT SHOCK PROTEIN); Molecular chaperone. Has ATPase activity.	0.843
GRPE	lon	WS0495	WS1972	GRPE PROTEIN (HSP-70 COFACTOR); 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 [...]	PUTATIVE ATP-DEPENDENT PROTEASE LA PROTEIN; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.	0.850
WS1291	era	WS1291	WS1292	CONSERVED HYPOTHETICAL SECRETED PROTEIN.	GTP-BINDING PROTEIN; An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.	0.779
WS1291	hslU	WS1291	WS1293	CONSERVED HYPOTHETICAL SECRETED PROTEIN.	CLPY PROTEIN; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.	0.779
WS1291	hslV	WS1291	WS1294	CONSERVED HYPOTHETICAL SECRETED PROTEIN.	HEAT SHOCK PROTEIN; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.734
dnaJ	GROEL	WS0698	WS0308	CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN DNAJ PROTEIN; 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-dependen [...]	HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.912