| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AS25_05365 | AS25_07960 | AS25_05365 | AS25_07960 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.536 |
| AS25_05365 | dnaJ | AS25_05365 | AS25_03885 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | 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, [...] | 0.510 |
| AS25_05365 | dnaK | AS25_05365 | AS25_07950 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.598 |
| AS25_05365 | fusA | AS25_05365 | AS25_00955 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | 0.636 |
| AS25_05365 | groEL | AS25_05365 | AS25_00640 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.722 |
| AS25_05365 | groEL-2 | AS25_05365 | AS25_07230 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.719 |
| AS25_05365 | groS | AS25_05365 | AS25_00645 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.489 |
| AS25_05365 | grpE | AS25_05365 | AS25_07955 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin 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 [...] | 0.488 |
| AS25_07960 | AS25_05365 | AS25_07960 | AS25_05365 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | 0.536 |
| AS25_07960 | dnaJ | AS25_07960 | AS25_03885 | Molecular chaperone DnaJ; 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, [...] | 0.412 |
| AS25_07960 | dnaK | AS25_07960 | AS25_07950 | Molecular chaperone DnaJ; 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. | 0.999 |
| AS25_07960 | fusA | AS25_07960 | AS25_00955 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | 0.621 |
| AS25_07960 | groEL | AS25_07960 | AS25_00640 | Molecular chaperone DnaJ; 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. | 0.860 |
| AS25_07960 | groEL-2 | AS25_07960 | AS25_07230 | Molecular chaperone DnaJ; 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. | 0.861 |
| AS25_07960 | groS | AS25_07960 | AS25_00645 | Molecular chaperone DnaJ; 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. | 0.795 |
| AS25_07960 | grpE | AS25_07960 | AS25_07955 | Molecular chaperone DnaJ; 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 [...] | 0.982 |
| AS25_07960 | guaB | AS25_07960 | AS25_13430 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Inosine-5-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.506 |
| dnaJ | AS25_05365 | AS25_03885 | AS25_05365 | 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, [...] | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | 0.510 |
| dnaJ | AS25_07960 | AS25_03885 | AS25_07960 | 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, [...] | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.412 |
| dnaJ | dnaK | AS25_03885 | AS25_07950 | 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, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |