| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ07142.1 | dnaJ | SKA53_02061 | SKA53_11638 | 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 [...] | 0.658 |
| EAQ07142.1 | grpE | SKA53_02061 | SKA53_11833 | 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 [...] | 0.666 |
| EAQ07142.1 | hslU | SKA53_02061 | SKA53_11943 | 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. | 0.720 |
| EAQ07142.1 | hslV | SKA53_02061 | SKA53_11953 | 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. | 0.813 |
| EAQ07539.1 | EAQ07753.1 | SKA53_11918 | SKA53_12988 | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | COG3118 Thioredoxin domain-containing protein. | 0.804 |
| EAQ07539.1 | grpE | SKA53_11918 | SKA53_11833 | 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 [...] | 0.414 |
| EAQ07539.1 | hslU | SKA53_11918 | SKA53_11943 | 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. | 0.543 |
| EAQ07539.1 | hslV | SKA53_11918 | SKA53_11953 | 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. | 0.807 |
| EAQ07545.1 | hslU | SKA53_11948 | SKA53_11943 | Hypothetical protein; COG0004 Ammonia permease. | 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. | 0.853 |
| EAQ07545.1 | hslV | SKA53_11948 | SKA53_11953 | Hypothetical protein; COG0004 Ammonia permease. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.853 |
| EAQ07753.1 | EAQ07539.1 | SKA53_12988 | SKA53_11918 | COG3118 Thioredoxin domain-containing protein. | FxsA; COG3030 Protein affecting phage T7 exclusion by the F plasmid. | 0.804 |
| EAQ07753.1 | dnaJ | SKA53_12988 | SKA53_11638 | 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 [...] | 0.720 |
| EAQ07753.1 | groEL | SKA53_12988 | SKA53_08666 | COG3118 Thioredoxin domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.877 |
| EAQ07753.1 | groS | SKA53_12988 | SKA53_08661 | 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. | 0.569 |
| EAQ07753.1 | grpE | SKA53_12988 | SKA53_11833 | 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 [...] | 0.893 |
| EAQ07753.1 | hslU | SKA53_12988 | SKA53_11943 | 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. | 0.870 |
| EAQ07753.1 | hslV | SKA53_12988 | SKA53_11953 | 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. | 0.885 |
| EAQ07753.1 | lon | SKA53_12988 | SKA53_02726 | COG3118 Thioredoxin domain-containing protein. | 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. | 0.574 |
| dnaJ | EAQ07142.1 | SKA53_11638 | SKA53_02061 | 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). | 0.658 |
| dnaJ | EAQ07753.1 | SKA53_11638 | SKA53_12988 | 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. | 0.720 |
