node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDF21129.1 | SDG43108.1 | SAMN04489759_101596 | SAMN04489759_107177 | Hypothetical chaperone protein. | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 0.997 |
SDF21129.1 | clpP | SAMN04489759_101596 | SAMN04489759_103320 | Hypothetical chaperone protein. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.855 |
SDF21129.1 | dnaJ | SAMN04489759_101596 | SAMN04489759_101464 | 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, [...] | 0.995 |
SDF21129.1 | groL | SAMN04489759_101596 | SAMN04489759_109175 | Hypothetical chaperone protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.976 |
SDF21129.1 | groS | SAMN04489759_101596 | SAMN04489759_109174 | Hypothetical chaperone protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.935 |
SDF21129.1 | grpE | SAMN04489759_101596 | SAMN04489759_101509 | 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 [...] | 0.991 |
SDF21129.1 | hslU | SAMN04489759_101596 | SAMN04489759_101531 | 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. | 0.774 |
SDF21129.1 | hslV | SAMN04489759_101596 | SAMN04489759_101532 | 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. | 0.700 |
SDG43108.1 | SDF21129.1 | SAMN04489759_107177 | SAMN04489759_101596 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | Hypothetical chaperone protein. | 0.997 |
SDG43108.1 | clpP | SAMN04489759_107177 | SAMN04489759_103320 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.543 |
SDG43108.1 | dnaJ | SAMN04489759_107177 | SAMN04489759_101464 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 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, [...] | 0.995 |
SDG43108.1 | dnaK | SAMN04489759_107177 | SAMN04489759_101463 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
SDG43108.1 | groL | SAMN04489759_107177 | SAMN04489759_109175 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.976 |
SDG43108.1 | groS | SAMN04489759_107177 | SAMN04489759_109174 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.914 |
SDG43108.1 | grpE | SAMN04489759_107177 | SAMN04489759_101509 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 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 |
SDG43108.1 | hslU | SAMN04489759_107177 | SAMN04489759_101531 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 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. | 0.896 |
SDG43108.1 | hslV | SAMN04489759_107177 | SAMN04489759_101532 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 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. | 0.904 |
clpP | SDF21129.1 | SAMN04489759_103320 | SAMN04489759_101596 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.855 |
clpP | SDG43108.1 | SAMN04489759_103320 | SAMN04489759_107177 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 0.543 |
clpP | dnaJ | SAMN04489759_103320 | SAMN04489759_101464 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 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, [...] | 0.666 |