hslU protein (Chelativorans sp. BNC1) - STRING interaction network

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Your Current Organism:

Chelativorans sp. BNC1

NCBI taxonomy Id: 266779
Other names: C. sp. BNC1, Mesorhizobium sp. BNC1

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Meso_3272	clpB	Meso_3272	Meso_2996	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	ATPase AAA-2; 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.	0.452
Meso_3272	dnaJ	Meso_3272	Meso_0680	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	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 [...]	0.709
Meso_3272	dnaK	Meso_3272	Meso_0679	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.531
Meso_3272	grpE	Meso_3272	Meso_4019	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	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 [...]	0.833
Meso_3272	hslU	Meso_3272	Meso_3490	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	Heat shock protein HslVU, ATPase 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.	0.796
Meso_3272	hslV	Meso_3272	Meso_3492	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	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.	0.813
Meso_3272	lon	Meso_3272	Meso_1171	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	ATP-dependent proteinase. Serine peptidase. MEROPS family S16; 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.	0.622
Meso_3377	clpB	Meso_3377	Meso_2996	PFAM: RNA-binding S4; KEGG: bmb:BruAb1_1753 S4 domain protein.	ATPase AAA-2; 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.	0.471
Meso_3377	dnaJ	Meso_3377	Meso_0680	PFAM: RNA-binding S4; KEGG: bmb:BruAb1_1753 S4 domain protein.	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 [...]	0.691
Meso_3377	grpE	Meso_3377	Meso_4019	PFAM: RNA-binding S4; KEGG: bmb:BruAb1_1753 S4 domain 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 [...]	0.627
Meso_3377	hslU	Meso_3377	Meso_3490	PFAM: RNA-binding S4; KEGG: bmb:BruAb1_1753 S4 domain protein.	Heat shock protein HslVU, ATPase 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.	0.722
Meso_3377	hslV	Meso_3377	Meso_3492	PFAM: RNA-binding S4; KEGG: bmb:BruAb1_1753 S4 domain 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.	0.703
Meso_3491	hslU	Meso_3491	Meso_3490	PFAM: GCN5-related N-acetyltransferase; KEGG: sme:SMc02576 hypothetical acetyltransferase protein.	Heat shock protein HslVU, ATPase 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.	0.846
Meso_3491	hslV	Meso_3491	Meso_3492	PFAM: GCN5-related N-acetyltransferase; KEGG: sme:SMc02576 hypothetical acetyltransferase 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.	0.838
clpB	Meso_3272	Meso_2996	Meso_3272	ATPase AAA-2; 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.	TIGRFAM: thioredoxin; PFAM: Tetratricopeptide TPR_4 Thioredoxin domain; KEGG: mlo:mll4432 thioredoxin.	0.452
clpB	Meso_3377	Meso_2996	Meso_3377	ATPase AAA-2; 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.	PFAM: RNA-binding S4; KEGG: bmb:BruAb1_1753 S4 domain protein.	0.471
clpB	clpX	Meso_2996	Meso_1170	ATPase AAA-2; 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 ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.	0.799
clpB	dnaJ	Meso_2996	Meso_0680	ATPase AAA-2; 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 [...]	0.869
clpB	dnaK	Meso_2996	Meso_0679	ATPase AAA-2; 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 DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.969
clpB	grpE	Meso_2996	Meso_4019	ATPase AAA-2; 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.	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 [...]	0.829