| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| IO99_09125 | IO99_12025 | IO99_09125 | IO99_12025 | RNA-binding protein S4; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp90; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.488 |
| IO99_09125 | grpE | IO99_09125 | IO99_00275 | RNA-binding protein S4; 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- [...] | 0.579 |
| IO99_09125 | hslO | IO99_09125 | IO99_18445 | RNA-binding protein S4; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.832 |
| IO99_12025 | IO99_09125 | IO99_12025 | IO99_09125 | Molecular chaperone Hsp90; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA-binding protein S4; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.488 |
| IO99_12025 | dnaK | IO99_12025 | IO99_00280 | Molecular chaperone Hsp90; 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. | 0.995 |
| IO99_12025 | groEL | IO99_12025 | IO99_03905 | Molecular chaperone Hsp90; 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. | 0.988 |
| IO99_12025 | groS | IO99_12025 | IO99_03910 | Molecular chaperone Hsp90; 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. | 0.913 |
| IO99_12025 | grpE | IO99_12025 | IO99_00275 | Molecular chaperone Hsp90; 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- [...] | 0.875 |
| IO99_12025 | hslO | IO99_12025 | IO99_18445 | Molecular chaperone Hsp90; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.553 |
| IO99_12025 | lon | IO99_12025 | IO99_18065 | Molecular chaperone Hsp90; 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. | 0.789 |
| IO99_18435 | IO99_18440 | IO99_18435 | IO99_18440 | Benzoate transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | SAM-dependent methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.557 |
| IO99_18435 | hslO | IO99_18435 | IO99_18445 | Benzoate transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.594 |
| IO99_18440 | IO99_18435 | IO99_18440 | IO99_18435 | SAM-dependent methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Benzoate transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.557 |
| IO99_18440 | hslO | IO99_18440 | IO99_18445 | SAM-dependent methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.825 |
| dnaK | IO99_12025 | IO99_00280 | IO99_12025 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone Hsp90; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.995 |
| dnaK | groEL | IO99_00280 | IO99_03905 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.996 |
| dnaK | groS | IO99_00280 | IO99_03910 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.990 |
| dnaK | grpE | IO99_00280 | IO99_00275 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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- [...] | 0.999 |
| dnaK | hslO | IO99_00280 | IO99_18445 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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. | 0.556 |
| dnaK | lon | IO99_00280 | IO99_18065 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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. | 0.939 |