node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFL61325.1 | SFL71347.1 | SAMN04487943_102455 | SAMN04487943_103237 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | Plasmid segregation protein ParM. | 0.974 |
SFL61325.1 | dnaJ | SAMN04487943_102455 | SAMN04487943_104104 | 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, [...] | 0.984 |
SFL61325.1 | dnaK | SAMN04487943_102455 | SAMN04487943_104103 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.974 |
SFL61325.1 | groL | SAMN04487943_102455 | SAMN04487943_108170 | 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. | 0.869 |
SFL61325.1 | groS | SAMN04487943_102455 | SAMN04487943_108171 | 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. | 0.789 |
SFL61325.1 | grpE | SAMN04487943_102455 | SAMN04487943_104102 | 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 [...] | 0.728 |
SFL61325.1 | hslU | SAMN04487943_102455 | SAMN04487943_11381 | 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. | 0.759 |
SFL61325.1 | hslV | SAMN04487943_102455 | SAMN04487943_11382 | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.783 |
SFL71347.1 | SFL61325.1 | SAMN04487943_103237 | SAMN04487943_102455 | Plasmid segregation protein ParM. | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 0.974 |
SFL71347.1 | dnaJ | SAMN04487943_103237 | SAMN04487943_104104 | Plasmid segregation protein ParM. | 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, [...] | 0.994 |
SFL71347.1 | groL | SAMN04487943_103237 | SAMN04487943_108170 | Plasmid segregation protein ParM. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.930 |
SFL71347.1 | groS | SAMN04487943_103237 | SAMN04487943_108171 | Plasmid segregation protein ParM. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.879 |
SFL71347.1 | grpE | SAMN04487943_103237 | SAMN04487943_104102 | Plasmid segregation protein ParM. | 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 [...] | 0.982 |
SFL71347.1 | hslU | SAMN04487943_103237 | SAMN04487943_11381 | Plasmid segregation protein ParM. | 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. | 0.551 |
SFL71347.1 | hslV | SAMN04487943_103237 | SAMN04487943_11382 | Plasmid segregation protein ParM. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.532 |
SFL71347.1 | htpG | SAMN04487943_103237 | SAMN04487943_106224 | Plasmid segregation protein ParM. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.974 |
dnaJ | SFL61325.1 | SAMN04487943_104104 | SAMN04487943_102455 | 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, [...] | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase. | 0.984 |
dnaJ | SFL71347.1 | SAMN04487943_104104 | SAMN04487943_103237 | 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, [...] | Plasmid segregation protein ParM. | 0.994 |
dnaJ | dnaK | SAMN04487943_104104 | SAMN04487943_104103 | 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, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groL | SAMN04487943_104104 | SAMN04487943_108170 | 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, [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.915 |