| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DR97_77 | clpA | DR97_77 | DR97_5342 | Lon 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 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | 0.775 |
| DR97_77 | clpB | DR97_77 | DR97_1845 | Lon 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 | Chaperone protein ClpB; 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 | 0.813 |
| DR97_77 | clpB1 | DR97_77 | DR97_3426 | Lon 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 | annotation not available | 0.631 |
| DR97_77 | clpP2 | DR97_77 | DR97_4601 | Lon 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 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins; Belongs to the peptidase S14 family | 0.879 |
| DR97_77 | clpV1-1 | DR97_77 | DR97_3047 | Lon 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 | VI_ClpV1: type VI secretion ATPase, ClpV1 family | 0.433 |
| DR97_77 | clpX | DR97_77 | DR97_78 | Lon 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 | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP | 0.990 |
| DR97_77 | dnaK | DR97_77 | DR97_2105 | Lon 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 | Chaperone protein DnaK; Acts as a chaperone | 0.858 |
| DR97_77 | groL | DR97_77 | DR97_1563 | Lon 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 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.574 |
| DR97_77 | groS | DR97_77 | DR97_1564 | Lon 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 | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter | 0.578 |
| clpA | DR97_77 | DR97_5342 | DR97_77 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | Lon 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 | 0.775 |
| clpA | clpP2 | DR97_5342 | DR97_4601 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins; Belongs to the peptidase S14 family | 0.925 |
| clpA | clpX | DR97_5342 | DR97_78 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP | 0.945 |
| clpA | dnaK | DR97_5342 | DR97_2105 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | Chaperone protein DnaK; Acts as a chaperone | 0.806 |
| clpA | groL | DR97_5342 | DR97_1563 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.672 |
| clpA | groS | DR97_5342 | DR97_1564 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter | 0.645 |
| clpA | lon2 | DR97_5342 | DR97_1204 | clpA: ATP-dependent Clp protease ATP-binding subunit ClpA | Lon 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 | 0.631 |
| clpB | DR97_77 | DR97_1845 | DR97_77 | Chaperone protein ClpB; 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 | Lon 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 | 0.813 |
| clpB | clpP2 | DR97_1845 | DR97_4601 | Chaperone protein ClpB; 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 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins; Belongs to the peptidase S14 family | 0.858 |
| clpB | clpX | DR97_1845 | DR97_78 | Chaperone protein ClpB; 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 | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP | 0.821 |
| clpB | dnaK | DR97_1845 | DR97_2105 | Chaperone protein ClpB; 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 protein DnaK; Acts as a chaperone | 0.995 |
STRING Data Update
