| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADQ04108.1 | grpE | Calow_0525 | Calow_1330 | KEGG: ate:Athe_0649 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 [...] | 0.598 |
| ADQ04108.1 | hslO | Calow_0525 | Calow_0602 | KEGG: ate:Athe_0649 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. | 0.836 |
| ADQ04108.1 | hslU | Calow_0525 | Calow_1868 | KEGG: ate:Athe_0649 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.618 |
| ADQ04108.1 | hslV | Calow_0525 | Calow_1869 | KEGG: ate:Athe_0649 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.672 |
| ADQ04176.1 | ADQ04177.1 | Calow_0600 | Calow_0601 | PFAM: Methyltransferase type 12; KEGG: ate:Athe_0753 methyltransferase type 11. | KEGG: ate:Athe_0754 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | 0.601 |
| ADQ04176.1 | hslO | Calow_0600 | Calow_0602 | PFAM: Methyltransferase type 12; KEGG: ate:Athe_0753 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. | 0.523 |
| ADQ04177.1 | ADQ04176.1 | Calow_0601 | Calow_0600 | KEGG: ate:Athe_0754 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | PFAM: Methyltransferase type 12; KEGG: ate:Athe_0753 methyltransferase type 11. | 0.601 |
| ADQ04177.1 | dnaK | Calow_0601 | Calow_1329 | KEGG: ate:Athe_0754 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.530 |
| ADQ04177.1 | groL | Calow_0601 | Calow_1827 | KEGG: ate:Athe_0754 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.505 |
| ADQ04177.1 | grpE | Calow_0601 | Calow_1330 | KEGG: ate:Athe_0754 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock 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 [...] | 0.441 |
| ADQ04177.1 | hslO | Calow_0601 | Calow_0602 | KEGG: ate:Athe_0754 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. | 0.670 |
| dnaK | ADQ04177.1 | Calow_1329 | Calow_0601 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | KEGG: ate:Athe_0754 cold-shock DNA-binding domain protein; PFAM: Cold-shock protein DNA-binding; SMART: Cold shock protein. | 0.530 |
| dnaK | ftsH | Calow_1329 | Calow_0518 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.814 |
| dnaK | groL | Calow_1329 | Calow_1827 | 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. | 0.994 |
| dnaK | grpE | Calow_1329 | Calow_1330 | 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 [...] | 0.999 |
| dnaK | hslO | Calow_1329 | Calow_0602 | 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. | 0.517 |
| dnaK | hslU | Calow_1329 | Calow_1868 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.729 |
| dnaK | hslV | Calow_1329 | Calow_1869 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.652 |
| dnaK | lon | Calow_1329 | Calow_0742 | 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. | 0.864 |
| ftsH | dnaK | Calow_0518 | Calow_1329 | ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.814 |
