node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dnaJ_1 | dnaK_1 | TM5383_01516 | TM5383_01517 | 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 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ_1 | dnaK_2 | TM5383_01516 | TM5383_01643 | 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 70. | 0.990 |
dnaJ_1 | groL | TM5383_01516 | TM5383_01750 | 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 [...] | Stress protein H5; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.948 |
dnaJ_1 | grpE | TM5383_01516 | TM5383_02715 | 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 [...] | 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 rounds of ATP-dependen [...] | 0.982 |
dnaJ_1 | nqo1_1 | TM5383_01516 | TM5383_00561 | 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 [...] | NADH-quinone oxidoreductase subunit 1. | 0.974 |
dnaJ_1 | rplM | TM5383_01516 | TM5383_00305 | 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 [...] | 50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.925 |
dnaJ_1 | rplN | TM5383_01516 | TM5383_01777 | 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; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.929 |
dnaJ_1 | rplO | TM5383_01516 | TM5383_01787 | 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 [...] | 50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.923 |
dnaJ_1 | rplQ | TM5383_01516 | TM5383_01793 | 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 [...] | 50S ribosomal protein L17. | 0.931 |
dnaJ_1 | sodB | TM5383_01516 | TM5383_02099 | 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 [...] | Superoxide dismutase [Fe]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.932 |
dnaK_1 | dnaJ_1 | TM5383_01517 | TM5383_01516 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 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 [...] | 0.999 |
dnaK_1 | groL | TM5383_01517 | TM5383_01750 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Stress protein H5; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.984 |
dnaK_1 | grpE | TM5383_01517 | TM5383_02715 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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 rounds of ATP-dependen [...] | 0.998 |
dnaK_1 | nqo1_1 | TM5383_01517 | TM5383_00561 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | NADH-quinone oxidoreductase subunit 1. | 0.411 |
dnaK_1 | rplM | TM5383_01517 | TM5383_00305 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.721 |
dnaK_1 | rplN | TM5383_01517 | TM5383_01777 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.849 |
dnaK_1 | rplO | TM5383_01517 | TM5383_01787 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 50S ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family. | 0.561 |
dnaK_1 | sodB | TM5383_01517 | TM5383_02099 | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Superoxide dismutase [Fe]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.412 |
dnaK_2 | dnaJ_1 | TM5383_01643 | TM5383_01516 | Heat shock protein 70. | 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 [...] | 0.990 |
dnaK_2 | groL | TM5383_01643 | TM5383_01750 | Heat shock protein 70. | Stress protein H5; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.931 |