| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGA85713.1 | AGA88048.1 | Psest_1149 | Psest_3559 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | 0.839 |
| AGA85713.1 | groL | Psest_1149 | Psest_1151 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.620 |
| AGA85713.1 | grpE | Psest_1149 | Psest_0963 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | Molecular chaperone GrpE (heat shock protein); 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. [...] | 0.473 |
| AGA85713.1 | hslU | Psest_1149 | Psest_3937 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.712 |
| AGA85713.1 | hslV | Psest_1149 | Psest_3936 | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.840 |
| AGA86565.1 | AGA86762.1 | Psest_2031 | Psest_2230 | PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase. | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, plant; glutathione-disulfide reductase, animal/bacterial. | 0.561 |
| AGA86565.1 | AGA88048.1 | Psest_2031 | Psest_3559 | PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase. | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | 0.825 |
| AGA86565.1 | dnaJ | Psest_2031 | Psest_0965 | PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase. | 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 [...] | 0.478 |
| AGA86762.1 | AGA86565.1 | Psest_2230 | Psest_2031 | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, plant; glutathione-disulfide reductase, animal/bacterial. | PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase. | 0.561 |
| AGA86762.1 | AGA88048.1 | Psest_2230 | Psest_3559 | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, plant; glutathione-disulfide reductase, animal/bacterial. | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | 0.968 |
| AGA86762.1 | groL | Psest_2230 | Psest_1151 | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, plant; glutathione-disulfide reductase, animal/bacterial. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.490 |
| AGA86762.1 | hslU | Psest_2230 | Psest_3937 | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, plant; glutathione-disulfide reductase, animal/bacterial. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.447 |
| AGA87238.1 | AGA88048.1 | Psest_2731 | Psest_3559 | Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | 0.797 |
| AGA87238.1 | grpE | Psest_2731 | Psest_0963 | Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | Molecular chaperone GrpE (heat shock protein); 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. [...] | 0.588 |
| AGA88048.1 | AGA85713.1 | Psest_3559 | Psest_1149 | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | Protein affecting phage T7 exclusion by the F plasmid; PFAM: FxsA cytoplasmic membrane protein. | 0.839 |
| AGA88048.1 | AGA86565.1 | Psest_3559 | Psest_2031 | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | PFAM: Pyridine nucleotide-disulphide oxidoreductase; TIGRFAM: thioredoxin-disulfide reductase. | 0.825 |
| AGA88048.1 | AGA86762.1 | Psest_3559 | Psest_2230 | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; TIGRFAM: glutathione-disulfide reductase, plant; glutathione-disulfide reductase, animal/bacterial. | 0.968 |
| AGA88048.1 | AGA87238.1 | Psest_3559 | Psest_2731 | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.797 |
| AGA88048.1 | dnaJ | Psest_3559 | Psest_0965 | PFAM: Thioredoxin; TIGRFAM: 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 [...] | 0.858 |
| AGA88048.1 | groL | Psest_3559 | Psest_1151 | PFAM: Thioredoxin; TIGRFAM: thioredoxin. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.919 |