node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDR71801.1 | SDR84997.1 | SAMN04489834_0042 | SAMN04489834_0376 | Phage shock protein PspC (stress-responsive transcriptional regulator). | Molecular chaperone DnaJ. | 0.962 |
SDR71801.1 | SDS50945.1 | SAMN04489834_0042 | SAMN04489834_1612 | Phage shock protein PspC (stress-responsive transcriptional regulator). | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.856 |
SDR71801.1 | clpP | SAMN04489834_0042 | SAMN04489834_1816 | Phage shock protein PspC (stress-responsive transcriptional regulator). | 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. | 0.523 |
SDR71801.1 | clpP-2 | SAMN04489834_0042 | SAMN04489834_1817 | Phage shock protein PspC (stress-responsive transcriptional regulator). | 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. | 0.523 |
SDR71801.1 | dnaJ | SAMN04489834_0042 | SAMN04489834_2330 | Phage shock protein PspC (stress-responsive transcriptional regulator). | Molecular chaperone 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, [...] | 0.962 |
SDR71801.1 | groL | SAMN04489834_0042 | SAMN04489834_3115 | Phage shock protein PspC (stress-responsive transcriptional regulator). | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.884 |
SDR71801.1 | groS | SAMN04489834_0042 | SAMN04489834_1025 | Phage shock protein PspC (stress-responsive transcriptional regulator). | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.832 |
SDR71801.1 | grpE | SAMN04489834_0042 | SAMN04489834_0375 | Phage shock protein PspC (stress-responsive transcriptional regulator). | Molecular chaperone 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 [...] | 0.970 |
SDR84997.1 | SDR71801.1 | SAMN04489834_0376 | SAMN04489834_0042 | Molecular chaperone DnaJ. | Phage shock protein PspC (stress-responsive transcriptional regulator). | 0.962 |
SDR84997.1 | SDS50945.1 | SAMN04489834_0376 | SAMN04489834_1612 | Molecular chaperone DnaJ. | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.669 |
SDR84997.1 | clpP | SAMN04489834_0376 | SAMN04489834_1816 | Molecular chaperone DnaJ. | 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. | 0.476 |
SDR84997.1 | clpP-2 | SAMN04489834_0376 | SAMN04489834_1817 | Molecular chaperone DnaJ. | 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. | 0.496 |
SDR84997.1 | dnaK | SAMN04489834_0376 | SAMN04489834_0374 | Molecular chaperone DnaJ. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
SDR84997.1 | groL | SAMN04489834_0376 | SAMN04489834_3115 | Molecular chaperone DnaJ. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.875 |
SDR84997.1 | groS | SAMN04489834_0376 | SAMN04489834_1025 | Molecular chaperone DnaJ. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.735 |
SDR84997.1 | grpE | SAMN04489834_0376 | SAMN04489834_0375 | Molecular chaperone DnaJ. | Molecular chaperone 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 [...] | 0.992 |
SDS50945.1 | SDR71801.1 | SAMN04489834_1612 | SAMN04489834_0042 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Phage shock protein PspC (stress-responsive transcriptional regulator). | 0.856 |
SDS50945.1 | SDR84997.1 | SAMN04489834_1612 | SAMN04489834_0376 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaJ. | 0.669 |
SDS50945.1 | clpP | SAMN04489834_1612 | SAMN04489834_1816 | ATP-dependent Clp protease ATP-binding subunit ClpC; 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. | 0.854 |
SDS50945.1 | clpP-2 | SAMN04489834_1612 | SAMN04489834_1817 | ATP-dependent Clp protease ATP-binding subunit ClpC; 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. | 0.858 |