| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dnaJ | dnaK | plu0580 | plu0579 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| dnaJ | grpE | plu0580 | plu3372 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | 0.975 |
| dnaJ | hslO | plu0580 | plu0099 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | 33 kDa chaperonin (Heat shock protein 33) (HSP33); 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. | 0.621 |
| dnaJ | hslR | plu0580 | plu0098 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | Heat shock protein 15 (HSP15); Belongs to the HSP15 family. | 0.554 |
| dnaJ | hslU | plu0580 | plu4763 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | ATP-dependent Hsl protease ATP-binding subunit HslU (heat shock 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. | 0.891 |
| dnaJ | hslV | plu0580 | plu4762 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | ATP-dependent protease HslV (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.835 |
| dnaJ | lon | plu0580 | plu3867 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | Endopeptidase La, DNA-binding, ATP-dependent protease; 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. | 0.832 |
| dnaJ | tig | plu0580 | plu3870 | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | Trigger factor (TF) (chaperone); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.433 |
| dnaK | dnaJ | plu0579 | plu0580 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | 0.998 |
| dnaK | grpE | plu0579 | plu3372 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | 0.976 |
| dnaK | hslO | plu0579 | plu0099 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 33 kDa chaperonin (Heat shock protein 33) (HSP33); 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. | 0.511 |
| dnaK | hslR | plu0579 | plu0098 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein 15 (HSP15); Belongs to the HSP15 family. | 0.470 |
| dnaK | hslU | plu0579 | plu4763 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent Hsl protease ATP-binding subunit HslU (heat shock 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. | 0.854 |
| dnaK | hslV | plu0579 | plu4762 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent protease HslV (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.853 |
| dnaK | lon | plu0579 | plu3867 | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Endopeptidase La, DNA-binding, ATP-dependent protease; 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. | 0.637 |
| grpE | dnaJ | plu3372 | plu0580 | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | Heat shock protein dnaJ (HSP40) (chaperone 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 [...] | 0.975 |
| grpE | dnaK | plu3372 | plu0579 | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | Chaperone protein (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.976 |
| grpE | hslO | plu3372 | plu0099 | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | 33 kDa chaperonin (Heat shock protein 33) (HSP33); 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. | 0.572 |
| grpE | hslR | plu3372 | plu0098 | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | Heat shock protein 15 (HSP15); Belongs to the HSP15 family. | 0.548 |
| grpE | hslU | plu3372 | plu4763 | GrpE protein (HSP-70 cofactor) (heat shock protein B25.3) (HSP24); 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 [...] | ATP-dependent Hsl protease ATP-binding subunit HslU (heat shock 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. | 0.885 |
STRING v12.5 is now available!
