| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| NOR53_192 | NOR53_237 | NOR53_192 | NOR53_237 | Hypothetical protein. | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | 0.400 |
| NOR53_192 | dnaJ | NOR53_192 | NOR53_409 | Hypothetical 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 [...] | 0.955 |
| NOR53_192 | groL | NOR53_192 | NOR53_35 | Hypothetical protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.919 |
| NOR53_192 | grpE | NOR53_192 | NOR53_401 | Hypothetical 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 [...] | 0.988 |
| NOR53_192 | hslU | NOR53_192 | NOR53_3368 | Hypothetical protein. | Heat shock protein HslVU, ATPase 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. | 0.597 |
| NOR53_192 | htpG | NOR53_192 | NOR53_839 | Hypothetical protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.995 |
| NOR53_192 | rplK | NOR53_192 | NOR53_37 | Hypothetical protein. | Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.486 |
| NOR53_237 | NOR53_192 | NOR53_237 | NOR53_192 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Hypothetical protein. | 0.400 |
| NOR53_237 | dapB | NOR53_237 | NOR53_133 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. | 0.789 |
| NOR53_237 | dnaJ | NOR53_237 | NOR53_409 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | 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 [...] | 0.952 |
| NOR53_237 | dnaK | NOR53_237 | NOR53_411 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.811 |
| NOR53_237 | groL | NOR53_237 | NOR53_35 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.677 |
| NOR53_237 | grpE | NOR53_237 | NOR53_401 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | 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 [...] | 0.922 |
| NOR53_237 | hslU | NOR53_237 | NOR53_3368 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Heat shock protein HslVU, ATPase 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. | 0.885 |
| NOR53_237 | htpG | NOR53_237 | NOR53_839 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.824 |
| dapB | NOR53_237 | NOR53_133 | NOR53_237 | Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | 0.789 |
| dapB | dnaJ | NOR53_133 | NOR53_409 | Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. | 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 [...] | 0.956 |
| dapB | dnaK | NOR53_133 | NOR53_411 | Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.607 |
| dapB | grpE | NOR53_133 | NOR53_401 | Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. | 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 [...] | 0.500 |
| dnaJ | NOR53_192 | NOR53_409 | NOR53_192 | 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 [...] | Hypothetical protein. | 0.955 |