| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SDW04119.1 | SDX26951.1 | SAMN04488041_101141 | SAMN04488041_105285 | DnaJ domain-containing protein. | Hypothetical chaperone protein. | 0.951 |
| SDW04119.1 | clpP | SAMN04488041_101141 | SAMN04488041_102555 | DnaJ domain-containing protein. | ATP-dependent Clp protease, protease subunit; 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. | 0.514 |
| SDW04119.1 | dnaK | SAMN04488041_101141 | SAMN04488041_105251 | DnaJ domain-containing protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.965 |
| SDW04119.1 | groL | SAMN04488041_101141 | SAMN04488041_101535 | DnaJ domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.800 |
| SDW04119.1 | groS | SAMN04488041_101141 | SAMN04488041_101536 | DnaJ domain-containing protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.666 |
| SDW04119.1 | grpE | SAMN04488041_101141 | SAMN04488041_105357 | 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 [...] | 0.897 |
| SDW04119.1 | hslU | SAMN04488041_101141 | SAMN04488041_105335 | 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. | 0.666 |
| SDW04119.1 | hslV | SAMN04488041_101141 | SAMN04488041_105334 | 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. | 0.564 |
| SDW04119.1 | lon | SAMN04488041_101141 | SAMN04488041_102434 | DnaJ domain-containing protein. | ATP-dependent Lon protease; 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. | 0.634 |
| SDX26951.1 | SDW04119.1 | SAMN04488041_105285 | SAMN04488041_101141 | Hypothetical chaperone protein. | DnaJ domain-containing protein. | 0.951 |
| SDX26951.1 | clpP | SAMN04488041_105285 | SAMN04488041_102555 | Hypothetical chaperone protein. | ATP-dependent Clp protease, protease subunit; 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. | 0.668 |
| SDX26951.1 | dnaJ | SAMN04488041_105285 | SAMN04488041_105252 | Hypothetical chaperone protein. | Molecular chaperone 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, [...] | 0.955 |
| SDX26951.1 | groL | SAMN04488041_105285 | SAMN04488041_101535 | Hypothetical chaperone protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.919 |
| SDX26951.1 | groS | SAMN04488041_105285 | SAMN04488041_101536 | Hypothetical chaperone protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.885 |
| SDX26951.1 | grpE | SAMN04488041_105285 | SAMN04488041_105357 | Hypothetical chaperone 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 [...] | 0.975 |
| SDX26951.1 | hslU | SAMN04488041_105285 | SAMN04488041_105335 | Hypothetical chaperone 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. | 0.593 |
| SDX26951.1 | hslV | SAMN04488041_105285 | SAMN04488041_105334 | Hypothetical chaperone 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. | 0.532 |
| SDX26951.1 | lon | SAMN04488041_105285 | SAMN04488041_102434 | Hypothetical chaperone protein. | ATP-dependent Lon protease; 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. | 0.628 |
| clpP | SDW04119.1 | SAMN04488041_102555 | SAMN04488041_101141 | ATP-dependent Clp protease, protease subunit; 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. | DnaJ domain-containing protein. | 0.514 |
| clpP | SDX26951.1 | SAMN04488041_102555 | SAMN04488041_105285 | ATP-dependent Clp protease, protease subunit; 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. | Hypothetical chaperone protein. | 0.668 |