| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CEL27604.1 | dnaJ | SRM1_00934 | SRM1_00810 | Glucosaminate ammonia-lyase. | 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 [...] | 0.497 |
| CEL27604.1 | garB | SRM1_00934 | SRM1_02867 | Glucosaminate ammonia-lyase. | Glutathione amide reductase; Maintains high levels of reduced glutathione. | 0.654 |
| CEL27604.1 | nrdA | SRM1_00934 | SRM1_04193 | Glucosaminate ammonia-lyase. | Ribonucleoside-diphosphate reductase 1 subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.417 |
| CEL27604.1 | trxA_2 | SRM1_00934 | SRM1_05115 | Glucosaminate ammonia-lyase. | Thioredoxin-1. | 0.817 |
| CEL31744.1 | prmA_2 | SRM1_05113 | SRM1_05114 | Hypothetical protein. | Ribosomal protein L11 methyltransferase. | 0.915 |
| CEL31744.1 | trxA_2 | SRM1_05113 | SRM1_05115 | Hypothetical protein. | Thioredoxin-1. | 0.814 |
| dnaJ | CEL27604.1 | SRM1_00810 | SRM1_00934 | 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 [...] | Glucosaminate ammonia-lyase. | 0.497 |
| dnaJ | groL | SRM1_00810 | SRM1_04436 | 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 [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.991 |
| dnaJ | grpE | SRM1_00810 | SRM1_00808 | 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 [...] | 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 [...] | 0.998 |
| dnaJ | hslU | SRM1_00810 | SRM1_00447 | 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 [...] | 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. | 0.969 |
| dnaJ | hslV | SRM1_00810 | SRM1_00448 | 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 [...] | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.953 |
| dnaJ | nrdA | SRM1_00810 | SRM1_04193 | 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 [...] | Ribonucleoside-diphosphate reductase 1 subunit alpha; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.566 |
| dnaJ | trxA_2 | SRM1_00810 | SRM1_05115 | 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-1. | 0.810 |
| garB | CEL27604.1 | SRM1_02867 | SRM1_00934 | Glutathione amide reductase; Maintains high levels of reduced glutathione. | Glucosaminate ammonia-lyase. | 0.654 |
| garB | groL | SRM1_02867 | SRM1_04436 | Glutathione amide reductase; Maintains high levels of reduced glutathione. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.482 |
| garB | trxA_2 | SRM1_02867 | SRM1_05115 | Glutathione amide reductase; Maintains high levels of reduced glutathione. | Thioredoxin-1. | 0.964 |
| groL | dnaJ | SRM1_04436 | SRM1_00810 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.991 |
| groL | garB | SRM1_04436 | SRM1_02867 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Glutathione amide reductase; Maintains high levels of reduced glutathione. | 0.482 |
| groL | grpE | SRM1_04436 | SRM1_00808 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.995 |
| groL | hslU | SRM1_04436 | SRM1_00447 | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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. | 0.955 |
