| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APL_1479 | APL_1482 | APL_1479 | APL_1482 | Thioredoxin-like protein. | Hybrid peroxiredoxin HyPrx5. | 0.726 |
| APL_1479 | dnaJ | APL_1479 | APL_1905 | Thioredoxin-like protein. | 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 [...] | 0.445 |
| APL_1479 | dsbD | APL_1479 | APL_1359 | Thioredoxin-like protein. | Thiol:disulfide interchange protein DsbD precursor; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.694 |
| APL_1479 | msrA | APL_1479 | APL_1024 | Thioredoxin-like protein. | Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.880 |
| APL_1482 | APL_1479 | APL_1482 | APL_1479 | Hybrid peroxiredoxin HyPrx5. | Thioredoxin-like protein. | 0.726 |
| APL_1482 | APL_2031 | APL_1482 | APL_2031 | Hybrid peroxiredoxin HyPrx5. | Hypothetical protein. | 0.435 |
| APL_1482 | dsbD | APL_1482 | APL_1359 | Hybrid peroxiredoxin HyPrx5. | Thiol:disulfide interchange protein DsbD precursor; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.421 |
| APL_1482 | dsbE | APL_1482 | APL_1514 | Hybrid peroxiredoxin HyPrx5. | Thiol:disulfide interchange protein DsbE. | 0.435 |
| APL_1482 | msrA | APL_1482 | APL_1024 | Hybrid peroxiredoxin HyPrx5. | Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.958 |
| APL_1482 | nrfX | APL_1482 | APL_1051 | Hybrid peroxiredoxin HyPrx5. | Disulfide bound formation protein E (dsbE). | 0.435 |
| APL_2031 | APL_1482 | APL_2031 | APL_1482 | Hypothetical protein. | Hybrid peroxiredoxin HyPrx5. | 0.435 |
| APL_2031 | dnaJ | APL_2031 | APL_1905 | Hypothetical protein. | 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 [...] | 0.438 |
| APL_2031 | dsbD | APL_2031 | APL_1359 | Hypothetical protein. | Thiol:disulfide interchange protein DsbD precursor; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. | 0.451 |
| APL_2031 | msrA | APL_2031 | APL_1024 | Hypothetical protein. | Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.854 |
| dnaJ | APL_1479 | APL_1905 | APL_1479 | 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-like protein. | 0.445 |
| dnaJ | APL_2031 | APL_1905 | APL_2031 | 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 [...] | Hypothetical protein. | 0.438 |
| dnaJ | dsbE | APL_1905 | APL_1514 | 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 [...] | Thiol:disulfide interchange protein DsbE. | 0.468 |
| dnaJ | grpE | APL_1905 | APL_0367 | 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 [...] | Heat shock protein (HSP-70 cofactor); 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 r [...] | 0.993 |
| dnaJ | msrA | APL_1905 | APL_1024 | 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 [...] | Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.859 |
| dnaJ | nrfX | APL_1905 | APL_1051 | 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 [...] | Disulfide bound formation protein E (dsbE). | 0.468 |
