| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB82962.1 | AEB82963.1 | Alide2_0546 | Alide2_0547 | KEGG: ajs:Ajs_3698 DnaK-related protein. | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | 0.808 |
| AEB82962.1 | dnaJ | Alide2_0546 | Alide2_1320 | KEGG: ajs:Ajs_3698 DnaK-related 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 [...] | 0.927 |
| AEB82962.1 | groL | Alide2_0546 | Alide2_0774 | KEGG: ajs:Ajs_3698 DnaK-related protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.860 |
| AEB82962.1 | grpE | Alide2_0546 | Alide2_1322 | KEGG: ajs:Ajs_3698 DnaK-related protein. | GrpE protein; 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-dependent i [...] | 0.921 |
| AEB82962.1 | hslU | Alide2_0546 | Alide2_4069 | KEGG: ajs:Ajs_3698 DnaK-related 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. | 0.634 |
| AEB82962.1 | htpG | Alide2_0546 | Alide2_0508 | KEGG: ajs:Ajs_3698 DnaK-related protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.947 |
| AEB82963.1 | AEB82962.1 | Alide2_0547 | Alide2_0546 | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | KEGG: ajs:Ajs_3698 DnaK-related protein. | 0.808 |
| AEB82963.1 | dnaJ | Alide2_0547 | Alide2_1320 | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 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 [...] | 0.927 |
| AEB82963.1 | groL | Alide2_0547 | Alide2_0774 | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.860 |
| AEB82963.1 | grpE | Alide2_0547 | Alide2_1322 | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | GrpE protein; 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-dependent i [...] | 0.921 |
| AEB82963.1 | hslU | Alide2_0547 | Alide2_4069 | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | 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. | 0.634 |
| AEB82963.1 | htpG | Alide2_0547 | Alide2_0508 | KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.947 |
| AEB85116.1 | dnaJ | Alide2_2765 | Alide2_1320 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 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 [...] | 0.868 |
| AEB85116.1 | groL | Alide2_2765 | Alide2_0774 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.846 |
| AEB85116.1 | grpE | Alide2_2765 | Alide2_1322 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein. | GrpE protein; 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-dependent i [...] | 0.915 |
| AEB85116.1 | hslU | Alide2_2765 | Alide2_4069 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 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. | 0.473 |
| AEB85116.1 | htpG | Alide2_2765 | Alide2_0508 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.936 |
| AEB85624.1 | dnaJ | Alide2_3283 | Alide2_1320 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 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 [...] | 0.868 |
| AEB85624.1 | groL | Alide2_3283 | Alide2_0774 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.846 |
| AEB85624.1 | grpE | Alide2_3283 | Alide2_1322 | PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein. | GrpE protein; 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-dependent i [...] | 0.915 |
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