| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SCL56177.1 | clpX | GA0070617_3163 | GA0070617_4672 | Clp amino terminal domain-containing protein, pathogenicity island component. | 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. | 0.425 |
| SCL56177.1 | groL | GA0070617_3163 | GA0070617_5104 | Clp amino terminal domain-containing protein, pathogenicity island component. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.617 |
| SCL56177.1 | groL-2 | GA0070617_3163 | GA0070617_5422 | Clp amino terminal domain-containing protein, pathogenicity island component. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.617 |
| SCL56177.1 | grpE | GA0070617_3163 | GA0070617_0279 | Clp amino terminal domain-containing protein, pathogenicity island component. | 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 [...] | 0.876 |
| SCL56177.1 | htpG | GA0070617_3163 | GA0070617_3584 | Clp amino terminal domain-containing protein, pathogenicity island component. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.724 |
| SCL56177.1 | lon | GA0070617_3163 | GA0070617_3255 | Clp amino terminal domain-containing protein, pathogenicity island component. | ATP-dependent Lon protease; 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. | 0.671 |
| SCL56999.1 | clpX | GA0070617_3405 | GA0070617_4672 | ATP-dependent Clp protease ATP-binding subunit ClpC; 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. | 0.425 |
| SCL56999.1 | ftsH | GA0070617_3405 | GA0070617_5615 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Cell division protease FtsH; 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; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.458 |
| SCL56999.1 | groL | GA0070617_3405 | GA0070617_5104 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.617 |
| SCL56999.1 | groL-2 | GA0070617_3405 | GA0070617_5422 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.617 |
| SCL56999.1 | grpE | GA0070617_3405 | GA0070617_0279 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 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 [...] | 0.876 |
| SCL56999.1 | htpG | GA0070617_3405 | GA0070617_3584 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.724 |
| SCL56999.1 | lon | GA0070617_3405 | GA0070617_3255 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | ATP-dependent Lon protease; 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. | 0.671 |
| SCL64827.1 | clpX | GA0070617_5578 | GA0070617_4672 | ATP-dependent Clp protease ATP-binding subunit ClpC; 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. | 0.425 |
| SCL64827.1 | ftsH | GA0070617_5578 | GA0070617_5615 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Cell division protease FtsH; 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; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.441 |
| SCL64827.1 | groL | GA0070617_5578 | GA0070617_5104 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.617 |
| SCL64827.1 | groL-2 | GA0070617_5578 | GA0070617_5422 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.617 |
| SCL64827.1 | grpE | GA0070617_5578 | GA0070617_0279 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 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 [...] | 0.876 |
| SCL64827.1 | htpG | GA0070617_5578 | GA0070617_3584 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.724 |
| SCL64827.1 | lon | GA0070617_5578 | GA0070617_3255 | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | ATP-dependent Lon protease; 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. | 0.671 |