| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rmet_1198 | clpP | Rmet_1198 | Rmet_1885 | Putative 20S proteasome, A and B subunits. | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. | 0.832 |
| Rmet_1198 | clpX | Rmet_1198 | Rmet_1884 | Putative 20S proteasome, A and B subunits. | ATPase and specificity subunit of ClpX-ClpP ATP-dependent 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. | 0.524 |
| Rmet_1198 | ftsH | Rmet_1198 | Rmet_2188 | Putative 20S proteasome, A and B subunits. | Protease, ATP-dependent zinc-metallo; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. | 0.423 |
| Rmet_1198 | groL | Rmet_1198 | Rmet_0616 | Putative 20S proteasome, A and B subunits. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.649 |
| Rmet_1198 | grpE | Rmet_1198 | Rmet_1004 | Putative 20S proteasome, A and B subunits. | Heat shock/stress protein; 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 AT [...] | 0.791 |
| Rmet_1198 | hslU | Rmet_1198 | Rmet_0132 | Putative 20S proteasome, A and B subunits. | Molecular chaperone and ATPase component of HslUV protease; 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. | 0.953 |
| Rmet_1198 | htpG | Rmet_1198 | Rmet_2506 | Putative 20S proteasome, A and B subunits. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.730 |
| Rmet_1198 | lon | Rmet_1198 | Rmet_1883 | Putative 20S proteasome, A and B subunits. | 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. | 0.624 |
| clpP | Rmet_1198 | Rmet_1885 | Rmet_1198 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. | Putative 20S proteasome, A and B subunits. | 0.832 |
| clpP | clpX | Rmet_1885 | Rmet_1884 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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 and specificity subunit of ClpX-ClpP ATP-dependent 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 | Rmet_1885 | Rmet_2921 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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 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 interaction [...] | 0.570 |
| clpP | ftsH | Rmet_1885 | Rmet_2188 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. | Protease, ATP-dependent zinc-metallo; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. | 0.467 |
| clpP | groL | Rmet_1885 | Rmet_0616 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.780 |
| clpP | grpE | Rmet_1885 | Rmet_1004 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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/stress protein; 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 AT [...] | 0.685 |
| clpP | hslU | Rmet_1885 | Rmet_0132 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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 and ATPase component of HslUV protease; 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. | 0.415 |
| clpP | hslV | Rmet_1885 | Rmet_0131 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. | 0.587 |
| clpP | htpG | Rmet_1885 | Rmet_2506 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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 HSP90 family; Molecular chaperone. Has ATPase activity. | 0.453 |
| clpP | lon | Rmet_1885 | Rmet_1883 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; 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. | 0.736 |
| clpX | Rmet_1198 | Rmet_1884 | Rmet_1198 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent 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. | Putative 20S proteasome, A and B subunits. | 0.524 |
| clpX | clpP | Rmet_1884 | Rmet_1885 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent 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 and ClpX-ClpP ATP-dependent serine proteases; 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 |