| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LDG_8725 | dnaJ | LDG_8725 | LDG_5101 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | 0.790 |
| LDG_8725 | dnaK | LDG_8725 | LDG_5102 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperone protein DnaK (heat shock 70 kDa protein,HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.536 |
| LDG_8725 | groL | LDG_8725 | LDG_6757 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.605 |
| LDG_8725 | groS | LDG_8725 | LDG_6756 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.419 |
| LDG_8725 | grpE | LDG_8725 | LDG_5103 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Heat-shock protein GrpE(HSP-70 cofactor); 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. Sever [...] | 0.699 |
| LDG_8725 | hslU | LDG_8725 | LDG_7364 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Hypothetical protein; 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. | 0.853 |
| LDG_8725 | hslV | LDG_8725 | LDG_7365 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.844 |
| LDG_8725 | htpG | LDG_8725 | LDG_5741 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.620 |
| LDG_8725 | lon | LDG_8725 | LDG_7721 | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | ATP-dependent protease La; 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. | 0.764 |
| dnaJ | LDG_8725 | LDG_5101 | LDG_8725 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.790 |
| dnaJ | dnaK | LDG_5101 | LDG_5102 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Chaperone protein DnaK (heat shock 70 kDa protein,HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | LDG_5101 | LDG_6757 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.978 |
| dnaJ | groS | LDG_5101 | LDG_6756 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.934 |
| dnaJ | grpE | LDG_5101 | LDG_5103 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Heat-shock protein GrpE(HSP-70 cofactor); 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. Sever [...] | 0.993 |
| dnaJ | hslU | LDG_5101 | LDG_7364 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Hypothetical protein; 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. | 0.956 |
| dnaJ | hslV | LDG_5101 | LDG_7365 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.951 |
| dnaJ | htpG | LDG_5101 | LDG_5741 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.983 |
| dnaJ | lon | LDG_5101 | LDG_7721 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | ATP-dependent protease La; 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. | 0.933 |
| dnaJ | rpoD | LDG_5101 | LDG_6611 | Chaperone protein DnaJ (heat shock protein); 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 interac [...] | RNA polymerase sigma 70 factor (RpoD); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth. | 0.737 |
| dnaK | LDG_8725 | LDG_5102 | LDG_8725 | Chaperone protein DnaK (heat shock 70 kDa protein,HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.536 |
