node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpB | dnaJ | XNC1_1283 | XNC1_0710 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | 0.701 |
clpB | dnaK | XNC1_1283 | XNC1_0708 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone Hsp70 in DNA biosynthesis/cell division; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.898 |
clpB | groS | XNC1_1283 | XNC1_3604 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone Hsp10 (GroES), part of GroE chaperone system; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.565 |
clpB | grpE | XNC1_1283 | XNC1_3251 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Hsp 24 nucleotide exchange factor; 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 roun [...] | 0.734 |
clpB | hscA | XNC1_1283 | XNC1_3302 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone (Hsp70 family), believed to be involved in assembly of Fe-S clusters; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | 0.783 |
clpB | hslU | XNC1_1283 | XNC1_0219 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.554 |
clpB | hslV | XNC1_1283 | XNC1_0220 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.530 |
clpB | htpG | XNC1_1283 | XNC1_0950 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.730 |
clpB | lon | XNC1_1283 | XNC1_0982 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Transposase (fragment); 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. | 0.569 |
clpB | ybbN | XNC1_1283 | XNC1_0930 | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Putative thioredoxin protein with protein prenylyltransferase. | 0.404 |
dnaJ | clpB | XNC1_0710 | XNC1_1283 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | ATP-dependent protease, Hsp 100, part of multi-chaperone system with DnaK, DnaJ, and GrpE; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.701 |
dnaJ | dnaK | XNC1_0710 | XNC1_0708 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Chaperone Hsp70 in DNA biosynthesis/cell division; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groS | XNC1_0710 | XNC1_3604 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Chaperone Hsp10 (GroES), part of GroE chaperone system; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.824 |
dnaJ | grpE | XNC1_0710 | XNC1_3251 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Hsp 24 nucleotide exchange factor; 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 roun [...] | 0.994 |
dnaJ | hscA | XNC1_0710 | XNC1_3302 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Chaperone (Hsp70 family), believed to be involved in assembly of Fe-S clusters; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | 0.993 |
dnaJ | hslU | XNC1_0710 | XNC1_0219 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.920 |
dnaJ | hslV | XNC1_0710 | XNC1_0220 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.850 |
dnaJ | htpG | XNC1_0710 | XNC1_0950 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.991 |
dnaJ | lon | XNC1_0710 | XNC1_0982 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Transposase (fragment); 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. | 0.860 |
dnaJ | ybbN | XNC1_0710 | XNC1_0930 | Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...] | Putative thioredoxin protein with protein prenylyltransferase. | 0.658 |