| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDR45946.1 | EDR46289.1 | DORFOR_02548 | DORFOR_02897 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | S4 domain protein; KEGG: bba:Bd3791 0.00031 rluD; pseudouridylate synthase K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 0.445 |
| EDR45946.1 | groL | DORFOR_02548 | DORFOR_00901 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.964 |
| EDR45946.1 | grpE | DORFOR_02548 | DORFOR_00807 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 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 [...] | 0.840 |
| EDR45946.1 | hslO | DORFOR_02548 | DORFOR_00817 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.477 |
| EDR46289.1 | EDR45946.1 | DORFOR_02897 | DORFOR_02548 | S4 domain protein; KEGG: bba:Bd3791 0.00031 rluD; pseudouridylate synthase K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.445 |
| EDR46289.1 | grpE | DORFOR_02897 | DORFOR_00807 | S4 domain protein; KEGG: bba:Bd3791 0.00031 rluD; pseudouridylate synthase K06180; COG: 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 [...] | 0.618 |
| EDR46289.1 | hslO | DORFOR_02897 | DORFOR_00817 | S4 domain protein; KEGG: bba:Bd3791 0.00031 rluD; pseudouridylate synthase K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.829 |
| EDR47737.1 | EDR47738.1 | DORFOR_00818 | DORFOR_00819 | Methyltransferase domain protein; KEGG: bce:BC4326 3.4e-44 methyltransferase K00599; COG: COG0500 SAM-dependent methyltransferases; Psort location: Cytoplasmic, score: 8.87. | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 0.466 |
| EDR47737.1 | hslO | DORFOR_00818 | DORFOR_00817 | Methyltransferase domain protein; KEGG: bce:BC4326 3.4e-44 methyltransferase K00599; COG: COG0500 SAM-dependent methyltransferases; Psort location: Cytoplasmic, score: 8.87. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.841 |
| EDR47737.1 | nadE | DORFOR_00818 | DORFOR_00816 | Methyltransferase domain protein; KEGG: bce:BC4326 3.4e-44 methyltransferase K00599; COG: COG0500 SAM-dependent methyltransferases; Psort location: Cytoplasmic, score: 8.87. | NAD+ synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.597 |
| EDR47738.1 | EDR47737.1 | DORFOR_00819 | DORFOR_00818 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Methyltransferase domain protein; KEGG: bce:BC4326 3.4e-44 methyltransferase K00599; COG: COG0500 SAM-dependent methyltransferases; Psort location: Cytoplasmic, score: 8.87. | 0.466 |
| EDR47738.1 | hslO | DORFOR_00819 | DORFOR_00817 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.466 |
| groL | EDR45946.1 | DORFOR_00901 | DORFOR_02548 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.964 |
| groL | grpE | DORFOR_00901 | DORFOR_00807 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.981 |
| groL | hslO | DORFOR_00901 | DORFOR_00817 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.520 |
| groL | nadE | DORFOR_00901 | DORFOR_00816 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | NAD+ synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.566 |
| grpE | EDR45946.1 | DORFOR_00807 | DORFOR_02548 | 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 [...] | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.840 |
| grpE | EDR46289.1 | DORFOR_00807 | DORFOR_02897 | 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 [...] | S4 domain protein; KEGG: bba:Bd3791 0.00031 rluD; pseudouridylate synthase K06180; COG: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog). | 0.618 |
| grpE | groL | DORFOR_00807 | DORFOR_00901 | 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 [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.981 |
| grpE | hslO | DORFOR_00807 | DORFOR_00817 | 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 [...] | Chaperonin HslO; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.573 |