node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHA_1312 | AHA_3746 | AHA_1312 | AHA_3746 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 0.625 |
AHA_1312 | dnaJ | AHA_1312 | AHA_2982 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | 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 [...] | 0.689 |
AHA_1312 | groL | AHA_1312 | AHA_0860 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.699 |
AHA_1312 | groS | AHA_1312 | AHA_0859 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.576 |
AHA_1312 | grpE | AHA_1312 | AHA_2984 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | 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 [...] | 0.772 |
AHA_1312 | hslU | AHA_1312 | AHA_4115 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | 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. | 0.797 |
AHA_1312 | hslV | AHA_1312 | AHA_4114 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.784 |
AHA_1312 | htpG | AHA_1312 | AHA_2490 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.756 |
AHA_1312 | lon | AHA_1312 | AHA_2013 | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | ATP-dependent protease La; 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. | 0.582 |
AHA_2582 | AHA_3746 | AHA_2582 | AHA_3746 | Conserved hypothetical protein. | DnaJ domain protein; Identified by match to protein family HMM PF00226. | 0.452 |
AHA_2582 | dnaJ | AHA_2582 | AHA_2982 | Conserved 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 [...] | 0.452 |
AHA_2582 | groL | AHA_2582 | AHA_0860 | Conserved hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.705 |
AHA_2582 | groS | AHA_2582 | AHA_0859 | Conserved hypothetical protein. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.492 |
AHA_2582 | grpE | AHA_2582 | AHA_2984 | Conserved 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 [...] | 0.699 |
AHA_2582 | hslU | AHA_2582 | AHA_4115 | Conserved 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. | 0.739 |
AHA_2582 | hslV | AHA_2582 | AHA_4114 | Conserved hypothetical protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.710 |
AHA_2582 | htpG | AHA_2582 | AHA_2490 | Conserved hypothetical protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.688 |
AHA_3746 | AHA_1312 | AHA_3746 | AHA_1312 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Thioredoxin domain protein; Identified by match to protein family HMM PF00085. | 0.625 |
AHA_3746 | AHA_2582 | AHA_3746 | AHA_2582 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Conserved hypothetical protein. | 0.452 |
AHA_3746 | groL | AHA_3746 | AHA_0860 | DnaJ domain protein; Identified by match to protein family HMM PF00226. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.784 |