| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dnaJ | dnaK | CBU_1289 | CBU_1290 | Chaperone 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 a [...] | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | 0.998 |
| dnaJ | groEL | CBU_1289 | CBU_1718 | Chaperone 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 a [...] | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.842 |
| dnaJ | groES | CBU_1289 | CBU_1719 | Chaperone 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 a [...] | 10 kDa chaperonin GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.867 |
| dnaJ | grpE | CBU_1289 | CBU_1293 | Chaperone 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 a [...] | GrpE; 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 interacti [...] | 0.982 |
| dnaJ | hslU | CBU_1289 | CBU_2012 | Chaperone 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 a [...] | ATP-dependent endopeptidase hsl ATP-binding 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. | 0.825 |
| dnaJ | hslV | CBU_1289 | CBU_2011 | Chaperone 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 a [...] | ATP-dependent endopeptidase hsl proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.795 |
| dnaJ | htpG | CBU_1289 | CBU_0309 | Chaperone 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 a [...] | Chaperone protein; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family. | 0.953 |
| dnaJ | lon | CBU_1289 | CBU_0740 | Chaperone 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 a [...] | ATP-dependent endopeptidase; 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. | 0.757 |
| dnaK | dnaJ | CBU_1290 | CBU_1289 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | Chaperone 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 a [...] | 0.998 |
| dnaK | groEL | CBU_1290 | CBU_1718 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.988 |
| dnaK | groES | CBU_1290 | CBU_1719 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | 10 kDa chaperonin GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.949 |
| dnaK | grpE | CBU_1290 | CBU_1293 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | GrpE; 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 interacti [...] | 0.999 |
| dnaK | hslU | CBU_1290 | CBU_2012 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | ATP-dependent endopeptidase hsl ATP-binding 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. | 0.743 |
| dnaK | hslV | CBU_1290 | CBU_2011 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | ATP-dependent endopeptidase hsl proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.719 |
| dnaK | htpG | CBU_1290 | CBU_0309 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | Chaperone protein; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family. | 0.996 |
| dnaK | lon | CBU_1290 | CBU_0740 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | ATP-dependent endopeptidase; 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. | 0.720 |
| dnaK | rpoB | CBU_1290 | CBU_0231 | Chaperone protein; Acts as a chaperone (By similarity). Might have a role in the infectious process. | DNA-directed RNA polymerase beta chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.727 |
| gltA | groEL | CBU_1410 | CBU_1718 | Citrate synthase. | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.827 |
| gltA | rpoB | CBU_1410 | CBU_0231 | Citrate synthase. | DNA-directed RNA polymerase beta chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.823 |
| groEL | dnaJ | CBU_1718 | CBU_1289 | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Chaperone 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 a [...] | 0.842 |
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