| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AMQ41191.1 | AMQ41613.1 | AMS64_01655 | AMS64_04050 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.846 |
| AMQ41191.1 | groEL | AMS64_01655 | AMS64_19780 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.936 |
| AMQ41191.1 | grpE | AMS64_01655 | AMS64_16505 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.960 |
| AMQ41191.1 | hslU | AMS64_01655 | AMS64_01535 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding 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. | 0.543 |
| AMQ41191.1 | hslV | AMS64_01655 | AMS64_01540 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.505 |
| AMQ41191.1 | htpG | AMS64_01655 | AMS64_07940 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.940 |
| AMQ41191.1 | lon | AMS64_01655 | AMS64_10840 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; 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. | 0.635 |
| AMQ41613.1 | AMQ41191.1 | AMS64_04050 | AMS64_01655 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.846 |
| AMQ41613.1 | AMQ42087.1 | AMS64_04050 | AMS64_06685 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| AMQ41613.1 | dnaK | AMS64_04050 | AMS64_16500 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.964 |
| AMQ41613.1 | groEL | AMS64_04050 | AMS64_19780 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.910 |
| AMQ41613.1 | grpE | AMS64_04050 | AMS64_16505 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.949 |
| AMQ41613.1 | hscA | AMS64_04050 | AMS64_11635 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.949 |
| AMQ41613.1 | hslU | AMS64_04050 | AMS64_01535 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease ATP-binding 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. | 0.860 |
| AMQ41613.1 | hslV | AMS64_04050 | AMS64_01540 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.840 |
| AMQ41613.1 | htpG | AMS64_04050 | AMS64_07940 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.960 |
| AMQ41613.1 | lon | AMS64_04050 | AMS64_10840 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; 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. | 0.852 |
| AMQ42087.1 | AMQ41613.1 | AMS64_06685 | AMS64_04050 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| AMQ42087.1 | groEL | AMS64_06685 | AMS64_19780 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.944 |
| AMQ42087.1 | grpE | AMS64_06685 | AMS64_16505 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.975 |
