| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKK67056.1 | dnaJ | FD63_05955 | FD63_08540 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 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, [...] | 0.993 |
| AKK67056.1 | groEL | FD63_05955 | FD63_17615 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; 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. | 0.926 |
| AKK67056.1 | groS | FD63_05955 | FD63_17620 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; 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. | 0.849 |
| AKK67056.1 | grpE | FD63_05955 | FD63_08530 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; 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- [...] | 0.971 |
| AKK67056.1 | hslU | FD63_05955 | FD63_03025 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 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. | 0.737 |
| AKK67056.1 | hslV | FD63_05955 | FD63_03020 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.667 |
| AKK67056.1 | htpG | FD63_05955 | FD63_07235 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.950 |
| AKK67056.1 | lon | FD63_05955 | FD63_04275 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 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. | 0.779 |
| AKK67056.1 | trxA-2 | FD63_05955 | FD63_06330 | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.420 |
| AKK68419.1 | dnaJ | FD63_13455 | FD63_08540 | 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; Belongs to the HSP33 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, [...] | 0.684 |
| AKK68419.1 | groEL | FD63_13455 | FD63_17615 | 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; Belongs to the HSP33 family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.519 |
| AKK68419.1 | grpE | FD63_13455 | FD63_08530 | 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; Belongs to the HSP33 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- [...] | 0.617 |
| AKK68419.1 | hslU | FD63_13455 | FD63_03025 | 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; Belongs to the HSP33 family. | 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. | 0.739 |
| AKK68419.1 | hslV | FD63_13455 | FD63_03020 | 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; Belongs to the HSP33 family. | Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.752 |
| AKK68419.1 | htpG | FD63_13455 | FD63_07235 | 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; Belongs to the HSP33 family. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.520 |
| AKK68419.1 | lon | FD63_13455 | FD63_04275 | 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; Belongs to the HSP33 family. | 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. | 0.601 |
| AKK68419.1 | trxA-2 | FD63_13455 | FD63_06330 | 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; Belongs to the HSP33 family. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.402 |
| dnaJ | AKK67056.1 | FD63_08540 | FD63_05955 | 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, [...] | 2-alkenal reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.993 |
| dnaJ | AKK68419.1 | FD63_08540 | FD63_13455 | 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, [...] | 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; Belongs to the HSP33 family. | 0.684 |
| dnaJ | groEL | FD63_08540 | FD63_17615 | 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 GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.979 |
