| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MICA_2325 | dnaK | MICA_2325 | MICA_1757 | Thioredoxin family protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.640 |
| MICA_2325 | groL | MICA_2325 | MICA_370 | Thioredoxin family protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.692 |
| MICA_2325 | grpE | MICA_2325 | MICA_1754 | Thioredoxin family protein. | grpE family 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-depe [...] | 0.870 |
| MICA_2325 | hslO | MICA_2325 | MICA_950 | Thioredoxin family protein. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.430 |
| MICA_2325 | htpG | MICA_2325 | MICA_794 | Thioredoxin family protein. | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase family protein; Molecular chaperone. Has ATPase activity. | 0.773 |
| MICA_2325 | lon | MICA_2325 | MICA_1381 | Thioredoxin family protein. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.574 |
| MICA_949 | MICA_951 | MICA_949 | MICA_951 | Putative uncharacterized protein. | Putative lipoprotein. | 0.529 |
| MICA_949 | hslO | MICA_949 | MICA_950 | Putative uncharacterized protein. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.623 |
| MICA_949 | topA | MICA_949 | MICA_1947 | Putative uncharacterized protein. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.579 |
| MICA_951 | MICA_949 | MICA_951 | MICA_949 | Putative lipoprotein. | Putative uncharacterized protein. | 0.529 |
| MICA_951 | hslO | MICA_951 | MICA_950 | Putative lipoprotein. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.741 |
| dnaK | MICA_2325 | MICA_1757 | MICA_2325 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Thioredoxin family protein. | 0.640 |
| dnaK | groL | MICA_1757 | MICA_370 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.978 |
| dnaK | grpE | MICA_1757 | MICA_1754 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | grpE family 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-depe [...] | 0.999 |
| dnaK | hslO | MICA_1757 | MICA_950 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.479 |
| dnaK | htpG | MICA_1757 | MICA_794 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase family protein; Molecular chaperone. Has ATPase activity. | 0.998 |
| dnaK | lon | MICA_1757 | MICA_1381 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.793 |
| dnaK | topA | MICA_1757 | MICA_1947 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.573 |
| groL | MICA_2325 | MICA_370 | MICA_2325 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin family protein. | 0.692 |
| groL | dnaK | MICA_370 | MICA_1757 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
STRING v12.5 is now available!
