| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJI79163.1 | clpC | CSING_08220 | CSING_11545 | Putative transcriptional regulator; PFAM: Helix-turn-helix domain. | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | 0.603 |
| AJI79163.1 | clpP2 | CSING_08220 | CSING_10460 | Putative transcriptional regulator; PFAM: Helix-turn-helix domain. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.634 |
| clpC | AJI79163.1 | CSING_11545 | CSING_08220 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Putative transcriptional regulator; PFAM: Helix-turn-helix domain. | 0.603 |
| clpC | clpP1 | CSING_11545 | CSING_10455 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.962 |
| clpC | clpP2 | CSING_11545 | CSING_10460 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.974 |
| clpC | clpS | CSING_11545 | CSING_10865 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.840 |
| clpC | clpX | CSING_11545 | CSING_10440 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB 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. | 0.718 |
| clpC | dnaJ1 | CSING_11545 | CSING_10030 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein DnaJ; 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 between DnaJ, D [...] | 0.712 |
| clpC | dnaJ2 | CSING_11545 | CSING_12005 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein DnaJ; 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 between DnaJ, D [...] | 0.712 |
| clpC | dnaK | CSING_11545 | CSING_12015 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.951 |
| clpC | groS | CSING_11545 | CSING_02665 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.686 |
| clpC | grpE | CSING_11545 | CSING_12010 | ATPase with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB 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. [...] | 0.887 |
| clpP1 | clpC | CSING_10455 | CSING_11545 | ATP-dependent Clp protease proteolytic subunit ClpP; 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 with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; UvrB/uvrC motif; ATPase family associated with various cellular activities (AAA); Belongs to the ClpA/ClpB family. | 0.962 |
| clpP1 | clpP2 | CSING_10455 | CSING_10460 | ATP-dependent Clp protease proteolytic subunit ClpP; 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 proteolytic subunit ClpP; 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 |
| clpP1 | clpS | CSING_10455 | CSING_10865 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | Hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.557 |
| clpP1 | clpX | CSING_10455 | CSING_10440 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.993 |
| clpP1 | dnaJ1 | CSING_10455 | CSING_10030 | ATP-dependent Clp protease proteolytic subunit ClpP; 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 DnaJ; 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 between DnaJ, D [...] | 0.403 |
| clpP1 | dnaJ2 | CSING_10455 | CSING_12005 | ATP-dependent Clp protease proteolytic subunit ClpP; 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 DnaJ; 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 between DnaJ, D [...] | 0.403 |
| clpP1 | dnaK | CSING_10455 | CSING_12015 | ATP-dependent Clp protease proteolytic subunit ClpP; 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; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.808 |
| clpP1 | groS | CSING_10455 | CSING_02665 | ATP-dependent Clp protease proteolytic subunit ClpP; 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-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.623 |