node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpQ | clpY | gene:10728362 | gene:10728361 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease (heat-shock protein); 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. | 0.999 |
clpQ | dnaJ | gene:10728362 | gene:10727242 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat-shock protein (activation of DnaK); 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 interaction [...] | 0.695 |
clpQ | dnaK | gene:10728362 | gene:10727240 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.665 |
clpQ | groEL | gene:10728362 | gene:10726431 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.777 |
clpQ | groES | gene:10728362 | gene:10726430 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.766 |
clpQ | grpE | gene:10728362 | gene:10727239 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat-shock protein (activation of DnaK); 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. Severa [...] | 0.860 |
clpQ | htpG | gene:10728362 | gene:10726901 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.845 |
clpQ | lonA | gene:10728362 | gene:10728960 | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent proteinase La 1 (lon) (class III heat-shock 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. | 0.804 |
clpY | clpQ | gene:10728361 | gene:10728362 | ATP-dependent Clp protease (heat-shock protein); 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. | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
clpY | dnaJ | gene:10728361 | gene:10727242 | ATP-dependent Clp protease (heat-shock protein); 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. | Heat-shock protein (activation of DnaK); 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 interaction [...] | 0.773 |
clpY | dnaK | gene:10728361 | gene:10727240 | ATP-dependent Clp protease (heat-shock protein); 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. | Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.721 |
clpY | groEL | gene:10728361 | gene:10726431 | ATP-dependent Clp protease (heat-shock protein); 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. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.855 |
clpY | groES | gene:10728361 | gene:10726430 | ATP-dependent Clp protease (heat-shock protein); 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. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.835 |
clpY | grpE | gene:10728361 | gene:10727239 | ATP-dependent Clp protease (heat-shock protein); 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. | Heat-shock protein (activation of DnaK); 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. Severa [...] | 0.895 |
clpY | htpG | gene:10728361 | gene:10726901 | ATP-dependent Clp protease (heat-shock protein); 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. | Class III heat-shock protein (chaperonin); Molecular chaperone. Has ATPase activity. | 0.832 |
clpY | lonA | gene:10728361 | gene:10728960 | ATP-dependent Clp protease (heat-shock protein); 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. | ATP-dependent proteinase La 1 (lon) (class III heat-shock 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. | 0.836 |
dnaJ | clpQ | gene:10727242 | gene:10728362 | Heat-shock protein (activation of DnaK); 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 interaction [...] | Beta-type subunit of the 20S proteasome; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.695 |
dnaJ | clpY | gene:10727242 | gene:10728361 | Heat-shock protein (activation of DnaK); 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 interaction [...] | ATP-dependent Clp protease (heat-shock protein); 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. | 0.773 |
dnaJ | dnaK | gene:10727242 | gene:10727240 | Heat-shock protein (activation of DnaK); 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 interaction [...] | Class I heat-shock protein (chaperonin); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groEL | gene:10727242 | gene:10726431 | Heat-shock protein (activation of DnaK); 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 interaction [...] | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.956 |