| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACP24399.1 | ACP24586.1 | NGR_c06060 | NGR_c07930 | long-chain-fatty-acid--CoA ligase. | Molecular chaperone, Hsp70 family. | 0.873 |
| ACP24399.1 | ACP26926.1 | NGR_c06060 | NGR_c31920 | long-chain-fatty-acid--CoA ligase. | Thioredoxin. | 0.430 |
| ACP24399.1 | dnaJ1 | NGR_c06060 | NGR_c35060 | long-chain-fatty-acid--CoA ligase. | 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 [...] | 0.916 |
| ACP24399.1 | dnaK2 | NGR_c06060 | NGR_c35070 | long-chain-fatty-acid--CoA ligase. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.873 |
| ACP24399.1 | groEL1 | NGR_c06060 | NGR_c04080 | long-chain-fatty-acid--CoA ligase. | 60 kDa chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.869 |
| ACP24399.1 | groEL2 | NGR_c06060 | NGR_c09450 | long-chain-fatty-acid--CoA ligase. | 60 kDa chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.869 |
| ACP24399.1 | groS | NGR_c06060 | NGR_c04090 | long-chain-fatty-acid--CoA ligase. | 10 kDa chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.470 |
| ACP24399.1 | grpE | NGR_c06060 | NGR_c00120 | long-chain-fatty-acid--CoA ligase. | 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 [...] | 0.400 |
| ACP24399.1 | lon | NGR_c06060 | NGR_c10370 | long-chain-fatty-acid--CoA ligase. | ATP-dependent protease La; 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. | 0.521 |
| ACP24586.1 | ACP24399.1 | NGR_c07930 | NGR_c06060 | Molecular chaperone, Hsp70 family. | long-chain-fatty-acid--CoA ligase. | 0.873 |
| ACP24586.1 | dnaJ1 | NGR_c07930 | NGR_c35060 | Molecular chaperone, Hsp70 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 [...] | 0.941 |
| ACP24586.1 | groEL1 | NGR_c07930 | NGR_c04080 | Molecular chaperone, Hsp70 family. | 60 kDa chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.943 |
| ACP24586.1 | groEL2 | NGR_c07930 | NGR_c09450 | Molecular chaperone, Hsp70 family. | 60 kDa chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.943 |
| ACP24586.1 | groS | NGR_c07930 | NGR_c04090 | Molecular chaperone, Hsp70 family. | 10 kDa chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.953 |
| ACP24586.1 | grpE | NGR_c07930 | NGR_c00120 | Molecular chaperone, Hsp70 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 [...] | 0.977 |
| ACP24586.1 | hslU | NGR_c07930 | NGR_c34070 | Molecular chaperone, Hsp70 family. | ATP-dependent Hsl 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. | 0.591 |
| ACP24586.1 | lon | NGR_c07930 | NGR_c10370 | Molecular chaperone, Hsp70 family. | ATP-dependent protease La; 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. | 0.794 |
| ACP26926.1 | ACP24399.1 | NGR_c31920 | NGR_c06060 | Thioredoxin. | long-chain-fatty-acid--CoA ligase. | 0.430 |
| ACP26926.1 | dnaJ1 | NGR_c31920 | NGR_c35060 | 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 [...] | 0.652 |
| ACP26926.1 | dnaK2 | NGR_c31920 | NGR_c35070 | Thioredoxin. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.557 |
