| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpP | clpQ | CDIV41_120070 | CDIV41_320318 | 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. | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.692 |
| clpP | clpY | CDIV41_120070 | CDIV41_320319 | 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. | Two-component ATP-dependent protease (ATPase and 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. | 0.607 |
| clpP | dnaJ | CDIV41_120070 | CDIV41_320455 | 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. | Co-factor of molecular chaperone; 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 interactions betwe [...] | 0.674 |
| clpP | dnaK | CDIV41_120070 | CDIV41_320456 | 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. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.715 |
| clpP | groEL | CDIV41_120070 | CDIV41_100004 | 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. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.775 |
| clpP | groES | CDIV41_120070 | CDIV41_100005 | 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. | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.837 |
| clpP | grpE | CDIV41_120070 | CDIV41_320457 | 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. | Protein GrpE; 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 rounds of ATP-dependent i [...] | 0.759 |
| clpP | hrcA | CDIV41_120070 | CDIV41_320458 | 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. | Transcriptional regulator of heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.620 |
| clpP | hslO | CDIV41_120070 | CDIV41_50004 | 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. | Disulfide bond chaperone (heat shock protein 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. | 0.464 |
| clpP | polA | CDIV41_120070 | CDIV41_320673 | 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. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.730 |
| clpQ | clpP | CDIV41_320318 | CDIV41_120070 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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. | 0.692 |
| clpQ | clpY | CDIV41_320318 | CDIV41_320319 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Two-component ATP-dependent protease (ATPase and 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. | 0.999 |
| clpQ | dnaJ | CDIV41_320318 | CDIV41_320455 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Co-factor of molecular chaperone; 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 interactions betwe [...] | 0.599 |
| clpQ | dnaK | CDIV41_320318 | CDIV41_320456 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.638 |
| clpQ | groEL | CDIV41_320318 | CDIV41_100004 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.698 |
| clpQ | groES | CDIV41_320318 | CDIV41_100005 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.639 |
| clpQ | grpE | CDIV41_320318 | CDIV41_320457 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Protein GrpE; 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 rounds of ATP-dependent i [...] | 0.764 |
| clpQ | hslO | CDIV41_320318 | CDIV41_50004 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Disulfide bond chaperone (heat shock protein 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. | 0.691 |
| clpY | clpP | CDIV41_320319 | CDIV41_120070 | Two-component ATP-dependent protease (ATPase and 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. | 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. | 0.607 |
| clpY | clpQ | CDIV41_320319 | CDIV41_320318 | Two-component ATP-dependent protease (ATPase and 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. | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
