node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MOC_1047 | MOC_3022 | MOC_1047 | MOC_3022 | Thioredoxin. | ATP-dependent Lon protease-like protein. | 0.683 |
MOC_1047 | dnaJ | MOC_1047 | MOC_4475 | 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 [...] | 0.849 |
MOC_1047 | dnaK | MOC_1047 | MOC_4474 | Thioredoxin. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.790 |
MOC_1047 | groL | MOC_1047 | MOC_4715 | Thioredoxin. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.741 |
MOC_1047 | groL-2 | MOC_1047 | MOC_0690 | Thioredoxin. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.741 |
MOC_1047 | grpE | MOC_1047 | MOC_4065 | Thioredoxin. | Heat shock protein 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- [...] | 0.902 |
MOC_1047 | hslU | MOC_1047 | MOC_3462 | Thioredoxin. | ATP-dependent 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. | 0.884 |
MOC_1047 | hslV | MOC_1047 | MOC_3458 | Thioredoxin. | ATP-dependent protease peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.874 |
MOC_1047 | htpG-2 | MOC_1047 | MOC_6045 | Thioredoxin. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.883 |
MOC_1047 | lon | MOC_1047 | MOC_5847 | Thioredoxin. | 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. | 0.683 |
MOC_3022 | MOC_1047 | MOC_3022 | MOC_1047 | ATP-dependent Lon protease-like protein. | Thioredoxin. | 0.683 |
MOC_3022 | dnaJ | MOC_3022 | MOC_4475 | ATP-dependent Lon protease-like 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 [...] | 0.848 |
MOC_3022 | dnaK | MOC_3022 | MOC_4474 | ATP-dependent Lon protease-like protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.819 |
MOC_3022 | groL | MOC_3022 | MOC_4715 | ATP-dependent Lon protease-like protein. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.792 |
MOC_3022 | groL-2 | MOC_3022 | MOC_0690 | ATP-dependent Lon protease-like protein. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.792 |
MOC_3022 | grpE | MOC_3022 | MOC_4065 | ATP-dependent Lon protease-like protein. | Heat shock protein 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- [...] | 0.844 |
MOC_3022 | hslU | MOC_3022 | MOC_3462 | ATP-dependent Lon protease-like protein. | ATP-dependent 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. | 0.856 |
MOC_3022 | hslV | MOC_3022 | MOC_3458 | ATP-dependent Lon protease-like protein. | ATP-dependent protease peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.834 |
MOC_3022 | htpG-2 | MOC_3022 | MOC_6045 | ATP-dependent Lon protease-like protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.853 |
dnaJ | MOC_1047 | MOC_4475 | MOC_1047 | 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 [...] | Thioredoxin. | 0.849 |