| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJF05460.1 | AJF06475.1 | GSUB_01110 | GSUB_07850 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 0.815 |
| AJF05460.1 | groEL | GSUB_01110 | GSUB_01520 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.772 |
| AJF05460.1 | groS | GSUB_01110 | GSUB_01525 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.668 |
| AJF05460.1 | grpE | GSUB_01110 | GSUB_00425 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 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- [...] | 0.900 |
| AJF05460.1 | hslU | GSUB_01110 | GSUB_03055 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent 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. | 0.620 |
| AJF05460.1 | hslV | GSUB_01110 | GSUB_03060 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.540 |
| AJF05460.1 | lon | GSUB_01110 | GSUB_15830 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; 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. | 0.592 |
| AJF06475.1 | AJF05460.1 | GSUB_07850 | GSUB_01110 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.815 |
| AJF06475.1 | clpX | GSUB_07850 | GSUB_06015 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Clp protease ATP-binding protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.434 |
| AJF06475.1 | dnaJ | GSUB_07850 | GSUB_00435 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 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, [...] | 0.960 |
| AJF06475.1 | groEL | GSUB_07850 | GSUB_01520 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.979 |
| AJF06475.1 | groS | GSUB_07850 | GSUB_01525 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.898 |
| AJF06475.1 | grpE | GSUB_07850 | GSUB_00425 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Heat shock protein 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- [...] | 0.861 |
| AJF06475.1 | hslO | GSUB_07850 | GSUB_00775 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Heat shock protein Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.467 |
| AJF06475.1 | hslU | GSUB_07850 | GSUB_03055 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | ATP-dependent 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. | 0.906 |
| AJF06475.1 | hslV | GSUB_07850 | GSUB_03060 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Hypothetical protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.915 |
| AJF06475.1 | lon | GSUB_07850 | GSUB_15830 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Peptidase; 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. | 0.824 |
| clpX | AJF06475.1 | GSUB_06015 | GSUB_07850 | Clp protease ATP-binding protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 0.434 |
| clpX | dnaJ | GSUB_06015 | GSUB_00435 | Clp protease ATP-binding protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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, [...] | 0.427 |
| clpX | groEL | GSUB_06015 | GSUB_01520 | Clp protease ATP-binding protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.722 |
