| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ05866.1 | EAQ08150.1 | SKA53_07167 | SKA53_10509 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | 0.991 |
| EAQ05866.1 | dnaK | SKA53_07167 | SKA53_11628 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.994 |
| EAQ05866.1 | groEL | SKA53_07167 | SKA53_08666 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.840 |
| EAQ05866.1 | groS | SKA53_07167 | SKA53_08661 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.667 |
| EAQ05866.1 | grpE | SKA53_07167 | SKA53_11833 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Co-chaperone 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-depend [...] | 0.936 |
| EAQ05866.1 | hrcA | SKA53_07167 | SKA53_11838 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.829 |
| EAQ05866.1 | hslU | SKA53_07167 | SKA53_11943 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | ATP-dependent protease 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. | 0.713 |
| EAQ05866.1 | hslV | SKA53_07167 | SKA53_11953 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.578 |
| EAQ05866.1 | lon | SKA53_07167 | SKA53_02726 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Probable ATP-dependent protease La 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. | 0.631 |
| EAQ08150.1 | EAQ05866.1 | SKA53_10509 | SKA53_07167 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 0.991 |
| EAQ08150.1 | dnaJ | SKA53_10509 | SKA53_11638 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Chaperone, 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, DnaK and [...] | 0.992 |
| EAQ08150.1 | groEL | SKA53_10509 | SKA53_08666 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.958 |
| EAQ08150.1 | groS | SKA53_10509 | SKA53_08661 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.926 |
| EAQ08150.1 | grpE | SKA53_10509 | SKA53_11833 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Co-chaperone 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-depend [...] | 0.994 |
| EAQ08150.1 | hrcA | SKA53_10509 | SKA53_11838 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.895 |
| EAQ08150.1 | hslU | SKA53_10509 | SKA53_11943 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | ATP-dependent protease 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. | 0.589 |
| EAQ08150.1 | hslV | SKA53_10509 | SKA53_11953 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.566 |
| EAQ08150.1 | lon | SKA53_10509 | SKA53_02726 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Probable ATP-dependent protease La 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. | 0.619 |
| dnaJ | EAQ08150.1 | SKA53_11638 | SKA53_10509 | Chaperone, 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, DnaK and [...] | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | 0.992 |
| dnaJ | dnaK | SKA53_11638 | SKA53_11628 | Chaperone, 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, DnaK and [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
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