| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SB4_08285 | SB4_08680 | SB4_08285 | SB4_08680 | Thioredoxin; 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. | 0.878 |
| SB4_08285 | dnaJ | SB4_08285 | SB4_07795 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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, [...] | 0.705 |
| SB4_08285 | dnaK | SB4_08285 | SB4_07800 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.559 |
| SB4_08285 | groEL | SB4_08285 | SB4_10950 | Thioredoxin; 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. | 0.894 |
| SB4_08285 | groS | SB4_08285 | SB4_10955 | Thioredoxin; 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. | 0.567 |
| SB4_08285 | grpE | SB4_08285 | SB4_07815 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.877 |
| SB4_08285 | hslV | SB4_08285 | SB4_08675 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.882 |
| SB4_08285 | lon | SB4_08285 | SB4_13845 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; 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. | 0.596 |
| SB4_08680 | SB4_08285 | SB4_08680 | SB4_08285 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.878 |
| SB4_08680 | SB4_16725 | SB4_08680 | SB4_16725 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone 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; Belongs to the HSP33 family. | 0.788 |
| SB4_08680 | clpX | SB4_08680 | SB4_13825 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone 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. | 0.752 |
| SB4_08680 | dnaJ | SB4_08680 | SB4_07795 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone 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, [...] | 0.937 |
| SB4_08680 | dnaK | SB4_08680 | SB4_07800 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.855 |
| SB4_08680 | groEL | SB4_08680 | SB4_10950 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.925 |
| SB4_08680 | groS | SB4_08680 | SB4_10955 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.912 |
| SB4_08680 | grpE | SB4_08680 | SB4_07815 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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 [...] | 0.931 |
| SB4_08680 | hslV | SB4_08680 | SB4_08675 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| SB4_08680 | lon | SB4_08680 | SB4_13845 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | DNA-binding protein; 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. | 0.892 |
| SB4_16725 | SB4_08680 | SB4_16725 | SB4_08680 | Molecular chaperone 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; Belongs to the HSP33 family. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.788 |
| SB4_16725 | clpX | SB4_16725 | SB4_13825 | Molecular chaperone 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; Belongs to the HSP33 family. | 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. | 0.437 |
