| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Cpap_0366 | Cpap_0367 | Cpap_0366 | Cpap_0367 | PFAM: Methyltransferase type 12; KEGG: cce:Ccel_2902 methyltransferase type 12. | KEGG: cce:Ccel_2901 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | 0.420 |
| Cpap_0366 | hslO | Cpap_0366 | Cpap_0368 | PFAM: Methyltransferase type 12; KEGG: cce:Ccel_2902 methyltransferase type 12. | 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. | 0.595 |
| Cpap_0367 | Cpap_0366 | Cpap_0367 | Cpap_0366 | KEGG: cce:Ccel_2901 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | PFAM: Methyltransferase type 12; KEGG: cce:Ccel_2902 methyltransferase type 12. | 0.420 |
| Cpap_0367 | hslO | Cpap_0367 | Cpap_0368 | KEGG: cce:Ccel_2901 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock 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. | 0.584 |
| Cpap_1088 | Cpap_2555 | Cpap_1088 | Cpap_2555 | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein. | KEGG: cce:Ccel_3084 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | 0.490 |
| Cpap_1088 | groL | Cpap_1088 | Cpap_2061 | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.941 |
| Cpap_1088 | groL-2 | Cpap_1088 | Cpap_3978 | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.941 |
| Cpap_1088 | grpE | Cpap_1088 | Cpap_3097 | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase 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 [...] | 0.919 |
| Cpap_1088 | hslO | Cpap_1088 | Cpap_0368 | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase 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. | 0.578 |
| Cpap_1088 | lon | Cpap_1088 | Cpap_2668 | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain 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. | 0.852 |
| Cpap_2555 | Cpap_1088 | Cpap_2555 | Cpap_1088 | KEGG: cce:Ccel_3084 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein. | 0.490 |
| Cpap_2555 | grpE | Cpap_2555 | Cpap_3097 | KEGG: cce:Ccel_3084 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding 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 [...] | 0.633 |
| Cpap_2555 | hslO | Cpap_2555 | Cpap_0368 | KEGG: cce:Ccel_3084 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding 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. | 0.875 |
| Cpap_2555 | lon | Cpap_2555 | Cpap_2668 | KEGG: cce:Ccel_3084 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain 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. | 0.435 |
| groL | Cpap_1088 | Cpap_2061 | Cpap_1088 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein. | 0.941 |
| groL | grpE | Cpap_2061 | Cpap_3097 | 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 [...] | 0.969 |
| groL | hslO | Cpap_2061 | Cpap_0368 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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. | 0.577 |
| groL | lon | Cpap_2061 | Cpap_2668 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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. | 0.741 |
| groL | msrA | Cpap_2061 | Cpap_0302 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Peptide methionine sulfoxide reductase; 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. | 0.536 |
| groL-2 | Cpap_1088 | Cpap_3978 | Cpap_1088 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | KEGG: cce:Ccel_0492 heat shock protein 90; PFAM: Heat shock protein Hsp90-like; ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein. | 0.941 |