| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FSU_0075 | FSU_2334 | FSU_0075 | FSU_2334 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | 0.551 |
| FSU_0075 | dnaJ | FSU_0075 | FSU_0184 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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 [...] | 0.811 |
| FSU_0075 | dnaK | FSU_0075 | FSU_0185 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.548 |
| FSU_0075 | groES | FSU_0075 | FSU_0455 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.500 |
| FSU_0075 | hepA | FSU_0075 | FSU_0598 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | RNA polymerase-associated protein HepA; Identified by similarity to SP:P23852; match to protein family HMM PF00176; match to protein family HMM PF00271. | 0.962 |
| FSU_0075 | htpG | FSU_0075 | FSU_0677 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.790 |
| FSU_2329 | FSU_2334 | FSU_2329 | FSU_2334 | Conserved domain protein; Identified by similarity to GB:BAC15296.1. | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | 0.497 |
| FSU_2329 | dnaJ | FSU_2329 | FSU_0184 | Conserved domain protein; Identified by similarity to GB:BAC15296.1. | 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 [...] | 0.816 |
| FSU_2329 | groEL | FSU_2329 | FSU_0456 | Conserved domain protein; Identified by similarity to GB:BAC15296.1. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.419 |
| FSU_2329 | hepA | FSU_2329 | FSU_0598 | Conserved domain protein; Identified by similarity to GB:BAC15296.1. | RNA polymerase-associated protein HepA; Identified by similarity to SP:P23852; match to protein family HMM PF00176; match to protein family HMM PF00271. | 0.770 |
| FSU_2329 | htpG | FSU_2329 | FSU_0677 | Conserved domain protein; Identified by similarity to GB:BAC15296.1. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.852 |
| FSU_2334 | FSU_0075 | FSU_2334 | FSU_0075 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.551 |
| FSU_2334 | FSU_2329 | FSU_2334 | FSU_2329 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | Conserved domain protein; Identified by similarity to GB:BAC15296.1. | 0.497 |
| FSU_2334 | dnaJ | FSU_2334 | FSU_0184 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | 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 [...] | 0.996 |
| FSU_2334 | groEL | FSU_2334 | FSU_0456 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
| FSU_2334 | groES | FSU_2334 | FSU_0455 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.914 |
| FSU_2334 | grpE | FSU_2334 | FSU_0193 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.992 |
| FSU_2334 | hepA | FSU_2334 | FSU_0598 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | RNA polymerase-associated protein HepA; Identified by similarity to SP:P23852; match to protein family HMM PF00176; match to protein family HMM PF00271. | 0.856 |
| FSU_2334 | htpG | FSU_2334 | FSU_0677 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.976 |
| FSU_2334 | lon | FSU_2334 | FSU_1853 | Putative chaperone protein DnaK; Identified by match to protein family HMM PF00012. | Identified by similarity to SP:P08177; match to protein family HMM PF00004; match to protein family HMM PF05362; match to protein family HMM PF07728; match to protein family HMM TIGR00763. | 0.748 |