node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GK0586 | clpQ | GK0586 | GK1213 | Hypothetical protein. | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.622 |
GK0586 | clpY | GK0586 | GK1214 | Hypothetical protein. | ATP-dependent Clp protease ATPase subunit; 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. | 0.721 |
GK0586 | dnaK | GK0586 | GK2504 | Hypothetical protein. | Chaperone protein (heat shock protein 70) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.984 |
GK0586 | groL | GK0586 | GK0249 | Hypothetical protein. | Chaperonin (GroEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
GK0586 | groS | GK0586 | GK0248 | Hypothetical protein. | Chaperonin (GroES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.689 |
GK0586 | grpE | GK0586 | GK2505 | Hypothetical protein. | Chaperone protein (heat shock 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 react [...] | 0.905 |
GK0586 | lon | GK0586 | GK2650 | Hypothetical protein. | ATP-dependent Lon protease; 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. | 0.700 |
clpQ | GK0586 | GK1213 | GK0586 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Hypothetical protein. | 0.622 |
clpQ | clpY | GK1213 | GK1214 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease ATPase subunit; 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 | GK1213 | GK2503 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone protein (heat shock 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 [...] | 0.622 |
clpQ | dnaK | GK1213 | GK2504 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone protein (heat shock protein 70) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.680 |
clpQ | groL | GK1213 | GK0249 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin (GroEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.832 |
clpQ | groS | GK1213 | GK0248 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin (GroES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.831 |
clpQ | grpE | GK1213 | GK2505 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone protein (heat shock 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 react [...] | 0.880 |
clpQ | lon | GK1213 | GK2650 | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Lon protease; 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. | 0.827 |
clpY | GK0586 | GK1214 | GK0586 | ATP-dependent Clp protease ATPase subunit; 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. | Hypothetical protein. | 0.721 |
clpY | clpQ | GK1214 | GK1213 | ATP-dependent Clp protease ATPase subunit; 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. | Proteasome Clp protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
clpY | dnaJ | GK1214 | GK2503 | ATP-dependent Clp protease ATPase subunit; 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. | Chaperone protein (heat shock 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 [...] | 0.721 |
clpY | dnaK | GK1214 | GK2504 | ATP-dependent Clp protease ATPase subunit; 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. | Chaperone protein (heat shock protein 70) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.737 |
clpY | groL | GK1214 | GK0249 | ATP-dependent Clp protease ATPase subunit; 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. | Chaperonin (GroEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.871 |