| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpP | clpX | HDEF_0809 | HDEF_0808 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.999 |
| clpP | dnaJ | HDEF_0809 | HDEF_0371 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 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 [...] | 0.582 |
| clpP | dnaK | HDEF_0809 | HDEF_0372 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | Chaperone Hsp70 in DNA biosynthesis/cell division; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.705 |
| clpP | groEL | HDEF_0809 | HDEF_0629 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | Chaperone Hsp60 (GroEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.765 |
| clpP | grpE | HDEF_0809 | HDEF_1754 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 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 [...] | 0.745 |
| clpP | hslU | HDEF_0809 | HDEF_1270 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 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. | 0.592 |
| clpP | hslV | HDEF_0809 | HDEF_1271 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.684 |
| clpP | lon | HDEF_0809 | HDEF_0807 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | DNA-binding 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. | 0.874 |
| clpP | mdh | HDEF_0809 | HDEF_0460 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | Malate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. | 0.593 |
| clpX | clpP | HDEF_0808 | HDEF_0809 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 0.999 |
| clpX | dnaJ | HDEF_0808 | HDEF_0371 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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 [...] | 0.590 |
| clpX | dnaK | HDEF_0808 | HDEF_0372 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Chaperone Hsp70 in DNA biosynthesis/cell division; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.677 |
| clpX | groEL | HDEF_0808 | HDEF_0629 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Chaperone Hsp60 (GroEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.732 |
| clpX | grpE | HDEF_0808 | HDEF_1754 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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 [...] | 0.604 |
| clpX | hslU | HDEF_0808 | HDEF_1270 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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. | 0.667 |
| clpX | hslV | HDEF_0808 | HDEF_1271 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.730 |
| clpX | lon | HDEF_0808 | HDEF_0807 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | DNA-binding 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. | 0.871 |
| clpX | mdh | HDEF_0808 | HDEF_0460 | ATPase, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Malate dehydrogenase, NAD(P)-binding; Catalyzes the reversible oxidation of malate to oxaloacetate. | 0.532 |
| dnaJ | clpP | HDEF_0371 | HDEF_0809 | 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 [...] | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 0.582 |
| dnaJ | clpX | HDEF_0371 | HDEF_0808 | 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, chaperone subunit of serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.590 |
