node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A7J50_0440 | A7J50_5201 | A7J50_0440 | A7J50_5201 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Thioredoxin; Pfam:pfam00085 Thioredoxin. | 0.702 |
A7J50_0440 | htpG | A7J50_0440 | A7J50_1964 | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.408 |
A7J50_2305 | A7J50_5201 | A7J50_2305 | A7J50_5201 | Thioredoxin reductase; Pfam:pfam07992 Pyridine nucleotide-disulphide oxidoreductase. | Thioredoxin; Pfam:pfam00085 Thioredoxin. | 0.657 |
A7J50_3023 | A7J50_5201 | A7J50_3023 | A7J50_5201 | Glutathione reductase; Maintains high levels of reduced glutathione. | Thioredoxin; Pfam:pfam00085 Thioredoxin. | 0.944 |
A7J50_4758 | A7J50_5201 | A7J50_4758 | A7J50_5201 | Exclusion suppressor FxsA; Pfam:pfam04186 FxsA cytoplasmic membrane protein. | Thioredoxin; Pfam:pfam00085 Thioredoxin. | 0.668 |
A7J50_4758 | hslU | A7J50_4758 | A7J50_0388 | Exclusion suppressor FxsA; Pfam:pfam04186 FxsA cytoplasmic membrane protein. | ATP-dependent protease ATPase subunit HslU; 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. | 0.482 |
A7J50_4758 | hslV | A7J50_4758 | A7J50_0389 | Exclusion suppressor FxsA; Pfam:pfam04186 FxsA cytoplasmic membrane protein. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.670 |
A7J50_4906 | A7J50_5201 | A7J50_4906 | A7J50_5201 | Thioredoxin reductase; Pfam:pfam07992 Pyridine nucleotide-disulphide oxidoreductase. | Thioredoxin; Pfam:pfam00085 Thioredoxin. | 0.672 |
A7J50_4906 | dnaJ | A7J50_4906 | A7J50_5014 | Thioredoxin reductase; Pfam:pfam07992 Pyridine nucleotide-disulphide oxidoreductase. | Chaperone protein 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, D [...] | 0.432 |
A7J50_5201 | A7J50_0440 | A7J50_5201 | A7J50_0440 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family. | 0.702 |
A7J50_5201 | A7J50_2305 | A7J50_5201 | A7J50_2305 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Thioredoxin reductase; Pfam:pfam07992 Pyridine nucleotide-disulphide oxidoreductase. | 0.657 |
A7J50_5201 | A7J50_3023 | A7J50_5201 | A7J50_3023 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Glutathione reductase; Maintains high levels of reduced glutathione. | 0.944 |
A7J50_5201 | A7J50_4758 | A7J50_5201 | A7J50_4758 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Exclusion suppressor FxsA; Pfam:pfam04186 FxsA cytoplasmic membrane protein. | 0.668 |
A7J50_5201 | A7J50_4906 | A7J50_5201 | A7J50_4906 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Thioredoxin reductase; Pfam:pfam07992 Pyridine nucleotide-disulphide oxidoreductase. | 0.672 |
A7J50_5201 | dnaJ | A7J50_5201 | A7J50_5014 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Chaperone protein 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, D [...] | 0.736 |
A7J50_5201 | grpE | A7J50_5201 | A7J50_5016 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | 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-dependent i [...] | 0.796 |
A7J50_5201 | hslU | A7J50_5201 | A7J50_0388 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | ATP-dependent protease ATPase subunit HslU; 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. | 0.821 |
A7J50_5201 | hslV | A7J50_5201 | A7J50_0389 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.813 |
A7J50_5201 | htpG | A7J50_5201 | A7J50_1964 | Thioredoxin; Pfam:pfam00085 Thioredoxin. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.713 |
dnaJ | A7J50_4906 | A7J50_5014 | A7J50_4906 | Chaperone protein 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, D [...] | Thioredoxin reductase; Pfam:pfam07992 Pyridine nucleotide-disulphide oxidoreductase. | 0.432 |