| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALO47927.1 | ALO49135.1 | AS203_01465 | AS203_08585 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.423 |
| ALO47927.1 | clpP | AS203_01465 | AS203_09360 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.421 |
| ALO47927.1 | dnaJ | AS203_01465 | AS203_09180 | 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, [...] | 0.473 |
| ALO47927.1 | dnaK | AS203_01465 | AS203_06930 | 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. | 0.551 |
| ALO47927.1 | groEL | AS203_01465 | AS203_05745 | 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. | 0.789 |
| ALO47927.1 | groS | AS203_01465 | AS203_05740 | 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. | 0.572 |
| ALO47927.1 | grpE | AS203_01465 | AS203_09185 | 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 [...] | 0.555 |
| ALO49135.1 | ALO47927.1 | AS203_08585 | AS203_01465 | Molecular chaperone HtpG; 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. | 0.423 |
| ALO49135.1 | ALO49180.1 | AS203_08585 | AS203_08840 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
| ALO49135.1 | clpP | AS203_08585 | AS203_09360 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.462 |
| ALO49135.1 | dnaJ | AS203_08585 | AS203_09180 | Molecular chaperone HtpG; 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, [...] | 0.864 |
| ALO49135.1 | dnaK | AS203_08585 | AS203_06930 | Molecular chaperone HtpG; 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. | 0.959 |
| ALO49135.1 | groEL | AS203_08585 | AS203_05745 | Molecular chaperone HtpG; 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. | 0.909 |
| ALO49135.1 | groS | AS203_08585 | AS203_05740 | Molecular chaperone HtpG; 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. | 0.789 |
| ALO49135.1 | grpE | AS203_08585 | AS203_09185 | Molecular chaperone HtpG; 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 [...] | 0.711 |
| ALO49135.1 | lon | AS203_08585 | AS203_08115 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.642 |
| ALO49180.1 | ALO49135.1 | AS203_08840 | AS203_08585 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
| ALO49180.1 | dnaJ | AS203_08840 | AS203_09180 | Hypothetical protein; 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, [...] | 0.794 |
| ALO49180.1 | groEL | AS203_08840 | AS203_05745 | Hypothetical 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. | 0.791 |
| ALO49180.1 | groS | AS203_08840 | AS203_05740 | Hypothetical 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. | 0.740 |