| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAR51206.1 | dnaJ | OG2516_15065 | OG2516_11106 | S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 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 [...] | 0.776 |
| EAR51206.1 | grpE | OG2516_15065 | OG2516_11351 | S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 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 [...] | 0.763 |
| EAR51206.1 | hslU | OG2516_15065 | OG2516_11241 | S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 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. | 0.786 |
| EAR51206.1 | hslV | OG2516_15065 | OG2516_11206 | S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.860 |
| EAR51206.1 | lon | OG2516_15065 | OG2516_03810 | S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 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. | 0.419 |
| EAR52920.1 | EAR53039.1 | OG2516_10671 | OG2516_11266 | COG3118 Thioredoxin domain-containing protein. | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | 0.860 |
| EAR52920.1 | dnaJ | OG2516_10671 | OG2516_11106 | COG3118 Thioredoxin domain-containing protein. | 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 [...] | 0.858 |
| EAR52920.1 | dnaK | OG2516_10671 | OG2516_11101 | COG3118 Thioredoxin domain-containing protein. | Heat shock protein (Hsp70, DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.759 |
| EAR52920.1 | groEL | OG2516_10671 | OG2516_17146 | COG3118 Thioredoxin domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.886 |
| EAR52920.1 | groS | OG2516_10671 | OG2516_17151 | COG3118 Thioredoxin domain-containing protein. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.696 |
| EAR52920.1 | grpE | OG2516_10671 | OG2516_11351 | COG3118 Thioredoxin domain-containing protein. | 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 [...] | 0.902 |
| EAR52920.1 | hslU | OG2516_10671 | OG2516_11241 | COG3118 Thioredoxin domain-containing protein. | 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. | 0.913 |
| EAR52920.1 | hslV | OG2516_10671 | OG2516_11206 | COG3118 Thioredoxin domain-containing protein. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.897 |
| EAR52920.1 | lon | OG2516_10671 | OG2516_03810 | COG3118 Thioredoxin domain-containing protein. | 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. | 0.770 |
| EAR53039.1 | EAR52920.1 | OG2516_11266 | OG2516_10671 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | COG3118 Thioredoxin domain-containing protein. | 0.860 |
| EAR53039.1 | grpE | OG2516_11266 | OG2516_11351 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | 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 [...] | 0.461 |
| EAR53039.1 | hslU | OG2516_11266 | OG2516_11241 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | 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. | 0.728 |
| EAR53039.1 | hslV | OG2516_11266 | OG2516_11206 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.861 |
| dnaJ | EAR51206.1 | OG2516_11106 | OG2516_15065 | 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 [...] | S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 0.776 |
| dnaJ | EAR52920.1 | OG2516_11106 | OG2516_10671 | 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 [...] | COG3118 Thioredoxin domain-containing protein. | 0.858 |
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