| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Cphy_0134 | Cphy_3369 | Cphy_0134 | Cphy_3369 | PFAM: RNA-binding S4 domain protein; KEGG: cpf:CPF_2801 S4 domain protein. | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | 0.508 |
| Cphy_0134 | grpE | Cphy_0134 | Cphy_2312 | PFAM: RNA-binding S4 domain protein; KEGG: cpf:CPF_2801 S4 domain protein. | 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 [...] | 0.611 |
| Cphy_0134 | hslO | Cphy_0134 | Cphy_3417 | PFAM: RNA-binding S4 domain protein; KEGG: cpf:CPF_2801 S4 domain protein. | Hsp33 protein; 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. | 0.862 |
| Cphy_3369 | Cphy_0134 | Cphy_3369 | Cphy_0134 | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | PFAM: RNA-binding S4 domain protein; KEGG: cpf:CPF_2801 S4 domain protein. | 0.508 |
| Cphy_3369 | dnaK | Cphy_3369 | Cphy_2311 | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
| Cphy_3369 | groL | Cphy_3369 | Cphy_3289 | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.975 |
| Cphy_3369 | grpE | Cphy_3369 | Cphy_2312 | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | 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 [...] | 0.854 |
| Cphy_3369 | hslO | Cphy_3369 | Cphy_3417 | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | Hsp33 protein; 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. | 0.525 |
| Cphy_3369 | lon | Cphy_3369 | Cphy_0379 | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | 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. | 0.830 |
| Cphy_3418 | hslO | Cphy_3418 | Cphy_3417 | PFAM: Methyltransferase type 11; Methyltransferase type 12; KEGG: cth:Cthe_1855 methyltransferase type 11. | Hsp33 protein; 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. | 0.757 |
| coaX | hslO | Cphy_0424 | Cphy_3417 | Putative transcriptional acitvator, Baf family; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis; Belongs to the type III pantothenate kinase family. | Hsp33 protein; 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. | 0.506 |
| dnaK | Cphy_3369 | Cphy_2311 | Cphy_3369 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | 0.996 |
| dnaK | groL | Cphy_2311 | Cphy_3289 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.996 |
| dnaK | grpE | Cphy_2311 | Cphy_2312 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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 [...] | 0.998 |
| dnaK | hslO | Cphy_2311 | Cphy_3417 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hsp33 protein; 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. | 0.515 |
| dnaK | lon | Cphy_2311 | Cphy_0379 | 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. | 0.933 |
| dnaK | topA | Cphy_2311 | Cphy_2722 | 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 [...] | 0.540 |
| groL | Cphy_3369 | Cphy_3289 | Cphy_3369 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | PFAM: heat shock protein Hsp90; KEGG: cth:Cthe_0550 heat shock protein HSP90. | 0.975 |
| groL | dnaK | Cphy_3289 | Cphy_2311 | Chaperonin GroEL; 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. | 0.996 |
| groL | grpE | Cphy_3289 | Cphy_2312 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.990 |