htpG protein (Xanthomonas campestris) - STRING interaction network

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htpG

Heat shock protein G; Molecular chaperone. Has ATPase activity. (634 aa)

Predicted Functional Partners:

dnaJ

0.955

dnaK

0.945

hsp90xc

0.941

groEL

0.893

cbpA

0.847

clpB

0.845

yegD

0.843

hslV

0.835

hslU

0.796

groES

0.785

Your Current Organism:

Xanthomonas campestris

NCBI taxonomy Id: 190485
Other names: X. campestris pv. campestris str. ATCC 33913, Xanthomonas campestris pv. campestris str. ATCC 33913

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
cbpA	clpB	XCC1048	XCC3070	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	0.699
cbpA	dnaK	XCC1048	XCC1474	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	DnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.975
cbpA	groEL	XCC1048	XCC0523	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	60kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.853
cbpA	groES	XCC1048	XCC0522	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	10kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.737
cbpA	hslU	XCC1048	XCC3493	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	ATP-dependent HslUV 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.	0.684
cbpA	hslV	XCC1048	XCC3494	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	ATP-dependent HslUV protease peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.606
cbpA	hsp90xc	XCC1048	XCC1168	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Hsp90xo protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.847
cbpA	htpG	XCC1048	XCC2393	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Heat shock protein G; Molecular chaperone. Has ATPase activity.	0.847
cbpA	yegD	XCC1048	XCC1309	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	Heat shock protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.882
clpB	cbpA	XCC3070	XCC1048	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	Curved DNA binding protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.699
clpB	dnaJ	XCC3070	XCC1475	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	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-dependent interactions between DnaJ, DnaK and Gr [...]	0.879
clpB	dnaK	XCC3070	XCC1474	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	DnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.935
clpB	groEL	XCC3070	XCC0523	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	60kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.677
clpB	groES	XCC3070	XCC0522	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	10kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.770
clpB	hslU	XCC3070	XCC3493	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	ATP-dependent HslUV 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.	0.766
clpB	hslV	XCC3070	XCC3494	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	ATP-dependent HslUV protease peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	0.526
clpB	hsp90xc	XCC3070	XCC1168	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	Hsp90xo protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.741
clpB	htpG	XCC3070	XCC2393	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	Heat shock protein G; Molecular chaperone. Has ATPase activity.	0.845
clpB	yegD	XCC3070	XCC1309	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	Heat shock protein; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.	0.863
dnaJ	clpB	XCC1475	XCC3070	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-dependent interactions between DnaJ, DnaK and Gr [...]	ATP-dependent Clp protease subunit; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to the ClpA/ClpB family.	0.879