| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCH85518.1 | clpP-3 | MODMU_0046 | MODMU_1709 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | 0.686 |
| CCH85518.1 | clpX | MODMU_0046 | MODMU_1710 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 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. | 0.483 |
| CCH85518.1 | groEL | MODMU_0046 | MODMU_0782 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.886 |
| CCH85518.1 | groL | MODMU_0046 | MODMU_4858 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.887 |
| CCH85518.1 | groS | MODMU_0046 | MODMU_4859 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 10kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.857 |
| CCH85518.1 | grpE | MODMU_0046 | MODMU_5178 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Molecular chaperone GrpE (Heat shock 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. [...] | 0.990 |
| CCH85518.1 | hrcA | MODMU_0046 | MODMU_1759 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Heat-inducible transcription repressor hrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.889 |
| CCH85518.1 | rplL | MODMU_0046 | MODMU_4932 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 50S ribosomal subunit protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family. | 0.423 |
| CCH85518.1 | tig | MODMU_0046 | MODMU_1707 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Peptidyl-prolyl cis/trans isomerase, Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.448 |
| clpP-3 | CCH85518.1 | MODMU_1709 | MODMU_0046 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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 heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.686 |
| clpP-3 | clpX | MODMU_1709 | MODMU_1710 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | 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. | 0.996 |
| clpP-3 | dnaK | MODMU_1709 | MODMU_5179 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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 protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.686 |
| clpP-3 | groEL | MODMU_1709 | MODMU_0782 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.726 |
| clpP-3 | groL | MODMU_1709 | MODMU_4858 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.725 |
| clpP-3 | groS | MODMU_1709 | MODMU_4859 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | 10kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.756 |
| clpP-3 | grpE | MODMU_1709 | MODMU_5178 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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 GrpE (Heat shock 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. [...] | 0.692 |
| clpP-3 | hrcA | MODMU_1709 | MODMU_1759 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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-inducible transcription repressor hrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.753 |
| clpP-3 | rplL | MODMU_1709 | MODMU_4932 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | 50S ribosomal subunit protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family. | 0.693 |
| clpP-3 | tig | MODMU_1709 | MODMU_1707 | ATP-dependent Clp protease proteolytic subunit (Endopeptidase Clp); 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. | Peptidyl-prolyl cis/trans isomerase, Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.796 |
| clpX | CCH85518.1 | MODMU_1710 | MODMU_0046 | 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. | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.483 |