node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dred_2498 | Dred_3116 | Dred_2498 | Dred_3116 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | Hypothetical protein. | 0.871 |
Dred_2498 | groS | Dred_2498 | Dred_2874 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.986 |
Dred_2498 | grpE | Dred_2498 | Dred_2497 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | 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 [...] | 0.987 |
Dred_2498 | hslU | Dred_2498 | Dred_1980 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | 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. | 0.792 |
Dred_2498 | hslV | Dred_2498 | Dred_1981 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | ATP dependent peptidase CodWX, CodW component, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.799 |
Dred_2498 | htpG | Dred_2498 | Dred_1472 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.903 |
Dred_2498 | lon | Dred_2498 | Dred_2559 | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | ATP-dependent proteinase, Serine peptidase, MEROPS family S16; 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. | 0.805 |
Dred_3116 | Dred_2498 | Dred_3116 | Dred_2498 | Hypothetical protein. | PFAM: chaperonin Cpn60/TCP-1; KEGG: chy:CHY_0413 thermosome, alpha subunit. | 0.871 |
Dred_3116 | groL | Dred_3116 | Dred_2873 | Hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.871 |
Dred_3116 | groS | Dred_3116 | Dred_2874 | Hypothetical protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.849 |
Dred_3116 | hslU | Dred_3116 | Dred_1980 | Hypothetical protein. | 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. | 0.802 |
Dred_3116 | hslV | Dred_3116 | Dred_1981 | Hypothetical protein. | ATP dependent peptidase CodWX, CodW component, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.793 |
Dred_3116 | htpG | Dred_3116 | Dred_1472 | Hypothetical protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.801 |
Dred_3116 | lon | Dred_3116 | Dred_2559 | Hypothetical protein. | ATP-dependent proteinase, Serine peptidase, MEROPS family S16; 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. | 0.795 |
codY | hslU | Dred_1979 | Dred_1980 | GTP-sensing transcriptional pleiotropic repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | 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. | 0.957 |
codY | hslV | Dred_1979 | Dred_1981 | GTP-sensing transcriptional pleiotropic repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | ATP dependent peptidase CodWX, CodW component, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.824 |
codY | xerC | Dred_1979 | Dred_1982 | GTP-sensing transcriptional pleiotropic repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | Tyrosine recombinase XerC subunit; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.613 |
groL | Dred_3116 | Dred_2873 | Dred_3116 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Hypothetical protein. | 0.871 |
groL | groS | Dred_2873 | Dred_2874 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
groL | grpE | Dred_2873 | Dred_2497 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.944 |