node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
FAES_0353 | FAES_1873 | FAES_0353 | FAES_1873 | DnaK-type molecular chaperone DnaK. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.988 |
FAES_0353 | clpP | FAES_0353 | FAES_4167 | DnaK-type molecular chaperone DnaK. | Endopeptidase Clp; 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. | 0.718 |
FAES_0353 | groL | FAES_0353 | FAES_2231 | DnaK-type molecular chaperone DnaK. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.922 |
FAES_0353 | groS | FAES_0353 | FAES_2230 | DnaK-type molecular chaperone DnaK. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.823 |
FAES_0353 | grpE | FAES_0353 | FAES_3095 | DnaK-type molecular chaperone DnaK. | 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 [...] | 0.980 |
FAES_0353 | hslU | FAES_0353 | FAES_4766 | DnaK-type molecular chaperone DnaK. | 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. | 0.584 |
FAES_0353 | hslV | FAES_0353 | FAES_2089 | DnaK-type molecular chaperone DnaK. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.577 |
FAES_1873 | FAES_0353 | FAES_1873 | FAES_0353 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | DnaK-type molecular chaperone DnaK. | 0.988 |
FAES_1873 | FAES_2125 | FAES_1873 | FAES_2125 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Hypothetical protein. | 0.987 |
FAES_1873 | clpP | FAES_1873 | FAES_4167 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Endopeptidase Clp; 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. | 0.425 |
FAES_1873 | dnaK-2 | FAES_1873 | FAES_4255 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.988 |
FAES_1873 | groL | FAES_1873 | FAES_2231 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.952 |
FAES_1873 | groS | FAES_1873 | FAES_2230 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.800 |
FAES_1873 | grpE | FAES_1873 | FAES_3095 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 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 [...] | 0.850 |
FAES_1873 | hslU | FAES_1873 | FAES_4766 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 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. | 0.862 |
FAES_1873 | hslV | FAES_1873 | FAES_2089 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.880 |
FAES_2125 | FAES_1873 | FAES_2125 | FAES_1873 | Hypothetical protein. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.987 |
FAES_2125 | clpP | FAES_2125 | FAES_4167 | Hypothetical protein. | Endopeptidase Clp; 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. | 0.646 |
FAES_2125 | groL | FAES_2125 | FAES_2231 | Hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.902 |
FAES_2125 | groS | FAES_2125 | FAES_2230 | Hypothetical protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.746 |