node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
RPA2546 | RPA2602 | RPA2546 | RPA2602 | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Peptidyl prolyl cis-trans isomerase; 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. | 0.565 |
RPA2546 | RPA3891 | RPA2546 | RPA3891 | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.515 |
RPA2546 | RPA4627 | RPA2546 | RPA4627 | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Conserved hypothetical protein; InterPro IPR001440 COGs COG0457. | 0.512 |
RPA2546 | dnaK | RPA2546 | RPA0333 | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.834 |
RPA2546 | htpG | RPA2546 | RPA4815 | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.905 |
RPA2602 | RPA2546 | RPA2602 | RPA2546 | Peptidyl prolyl cis-trans isomerase; 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. | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.565 |
RPA2602 | dnaJ | RPA2602 | RPA0334 | Peptidyl prolyl cis-trans isomerase; 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 DnaJ (40); 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 D [...] | 0.706 |
RPA2602 | dnaK | RPA2602 | RPA0333 | Peptidyl prolyl cis-trans isomerase; 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 DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.693 |
RPA2602 | htpG | RPA2602 | RPA4815 | Peptidyl prolyl cis-trans isomerase; 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. | 0.865 |
RPA3891 | RPA2546 | RPA3891 | RPA2546 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.515 |
RPA3891 | dnaJ | RPA3891 | RPA0334 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Heat shock protein DnaJ (40); 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 D [...] | 0.555 |
RPA3891 | dnaK | RPA3891 | RPA0333 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.962 |
RPA3891 | htpG | RPA3891 | RPA4815 | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.926 |
RPA4627 | RPA2546 | RPA4627 | RPA2546 | Conserved hypothetical protein; InterPro IPR001440 COGs COG0457. | FKBP-type peptidyl-prolyl cis-trans isomerase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.512 |
RPA4627 | dnaJ | RPA4627 | RPA0334 | Conserved hypothetical protein; InterPro IPR001440 COGs COG0457. | Heat shock protein DnaJ (40); 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 D [...] | 0.554 |
RPA4627 | dnaK | RPA4627 | RPA0333 | Conserved hypothetical protein; InterPro IPR001440 COGs COG0457. | Heat shock protein DnaK (70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.961 |
RPA4627 | htpG | RPA4627 | RPA4815 | Conserved hypothetical protein; InterPro IPR001440 COGs COG0457. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.925 |
dnaJ | RPA2602 | RPA0334 | RPA2602 | Heat shock protein DnaJ (40); 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 D [...] | Peptidyl prolyl cis-trans isomerase; 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. | 0.706 |
dnaJ | RPA3891 | RPA0334 | RPA3891 | Heat shock protein DnaJ (40); 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 D [...] | Unknown protein; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.555 |
dnaJ | RPA4627 | RPA0334 | RPA4627 | Heat shock protein DnaJ (40); 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 D [...] | Conserved hypothetical protein; InterPro IPR001440 COGs COG0457. | 0.554 |