| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EED32205.1 | NOR53_237 | NOR53_3624 | NOR53_237 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | 0.919 |
| EED32205.1 | NOR53_385 | NOR53_3624 | NOR53_385 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 20S proteasome, A/B subunit; [O] COG3484 Predicted proteasome-type protease. | 0.909 |
| EED32205.1 | clpP | NOR53_3624 | NOR53_2078 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.949 |
| EED32205.1 | clpX | NOR53_3624 | NOR53_1732 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.966 |
| EED32205.1 | dnaJ | NOR53_3624 | NOR53_409 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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 |
| EED32205.1 | groL | NOR53_3624 | NOR53_35 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.926 |
| EED32205.1 | groS | NOR53_3624 | NOR53_109 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.914 |
| EED32205.1 | grpE | NOR53_3624 | NOR53_401 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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 [...] | 0.967 |
| EED32205.1 | hslU | NOR53_3624 | NOR53_3368 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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. | 0.999 |
| EED32205.1 | htpG | NOR53_3624 | NOR53_839 | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.962 |
| NOR53_237 | EED32205.1 | NOR53_237 | NOR53_3624 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.919 |
| 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 [...] | 0.961 |
| 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. | 0.914 |
| NOR53_237 | groS | NOR53_237 | NOR53_109 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.594 |
| 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 [...] | 0.952 |
| 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. | 0.913 |
| NOR53_237 | htpG | NOR53_237 | NOR53_839 | Thioredoxin; [OC] COG0526 Thiol-disulfide isomerase and thioredoxins. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.836 |
| NOR53_385 | EED32205.1 | NOR53_385 | NOR53_3624 | 20S proteasome, A/B subunit; [O] COG3484 Predicted proteasome-type protease. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.909 |
| clpP | EED32205.1 | NOR53_2078 | NOR53_3624 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.949 |
| clpP | clpX | NOR53_2078 | NOR53_1732 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.999 |
