| 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 | clpX | CDIV41_120070 | CDIV41_320554 | 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 unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.998 |
| 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 | 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 | 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 |
| 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 | clpX | CDIV41_320318 | CDIV41_320554 | 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 unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.698 |
| 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 | codV | CDIV41_320318 | CDIV41_320317 | 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. | Site-specific tyrosine recombinase for chromosome partitioning; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.874 |
| clpQ | codY | CDIV41_320318 | CDIV41_320320 | 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. | Transcriptional regulator, GTP and BCAA-dependent; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | 0.826 |
| 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 |
| clpQ | trmFO | CDIV41_320318 | CDIV41_320316 | 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. | tRNA:m(5)U-54 methyltransferase; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. | 0.732 |
| clpX | clpP | CDIV41_320554 | CDIV41_120070 | Protein unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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. | 0.998 |
| clpX | clpQ | CDIV41_320554 | CDIV41_320318 | Protein unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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. | 0.698 |
| clpX | clpY | CDIV41_320554 | CDIV41_320319 | Protein unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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. | 0.689 |
