node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFR40876.1 | dnaK | SAMN04488073_0668 | SAMN04488073_1559 | DNA-J related protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.993 |
SFR40876.1 | groL | SAMN04488073_0668 | SAMN04488073_0901 | DNA-J related protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.867 |
SFR40876.1 | groS | SAMN04488073_0668 | SAMN04488073_0902 | DNA-J related protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.654 |
SFR40876.1 | grpE | SAMN04488073_0668 | SAMN04488073_1560 | DNA-J related protein. | 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 [...] | 0.903 |
SFR40876.1 | hslU | SAMN04488073_0668 | SAMN04488073_3313 | DNA-J related protein. | ATP-dependent HslUV 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. | 0.654 |
SFR40876.1 | hslV | SAMN04488073_0668 | SAMN04488073_3314 | DNA-J related protein. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.528 |
SFR40876.1 | htpG | SAMN04488073_0668 | SAMN04488073_0061 | DNA-J related protein. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.970 |
SFR43991.1 | dnaK | SAMN04488073_1265 | SAMN04488073_1559 | DnaJ domain-containing protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.993 |
SFR43991.1 | groL | SAMN04488073_1265 | SAMN04488073_0901 | DnaJ domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.867 |
SFR43991.1 | groS | SAMN04488073_1265 | SAMN04488073_0902 | DnaJ domain-containing protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.654 |
SFR43991.1 | grpE | SAMN04488073_1265 | SAMN04488073_1560 | DnaJ domain-containing protein. | 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 [...] | 0.903 |
SFR43991.1 | hslU | SAMN04488073_1265 | SAMN04488073_3313 | DnaJ domain-containing protein. | ATP-dependent HslUV 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. | 0.654 |
SFR43991.1 | hslV | SAMN04488073_1265 | SAMN04488073_3314 | DnaJ domain-containing protein. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.528 |
SFR43991.1 | htpG | SAMN04488073_1265 | SAMN04488073_0061 | DnaJ domain-containing protein. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.970 |
SFR44512.1 | dnaK | SAMN04488073_1350 | SAMN04488073_1559 | Curved DNA-binding protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
SFR44512.1 | groL | SAMN04488073_1350 | SAMN04488073_0901 | Curved DNA-binding protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.893 |
SFR44512.1 | groS | SAMN04488073_1350 | SAMN04488073_0902 | Curved DNA-binding protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.711 |
SFR44512.1 | grpE | SAMN04488073_1350 | SAMN04488073_1560 | Curved DNA-binding protein. | 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 [...] | 0.961 |
SFR44512.1 | hslU | SAMN04488073_1350 | SAMN04488073_3313 | Curved DNA-binding protein. | ATP-dependent HslUV 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. | 0.659 |
SFR44512.1 | hslV | SAMN04488073_1350 | SAMN04488073_3314 | Curved DNA-binding protein. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.528 |