node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABK47834.1 | ABK48671.1 | Shewana3_1600 | Shewana3_2442 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | 0.562 |
ABK47834.1 | clpP | Shewana3_1600 | Shewana3_2661 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.502 |
ABK47834.1 | groL | Shewana3_1600 | Shewana3_3567 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.796 |
ABK47834.1 | groS | Shewana3_1600 | Shewana3_3568 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.690 |
ABK47834.1 | grpE | Shewana3_1600 | Shewana3_2902 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ 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 [...] | 0.862 |
ABK47834.1 | hslU | Shewana3_1600 | Shewana3_3700 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ 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. | 0.756 |
ABK47834.1 | hslV | Shewana3_1600 | Shewana3_3699 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.707 |
ABK47834.1 | htpG | Shewana3_1600 | Shewana3_2443 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.935 |
ABK47834.1 | lon | Shewana3_1600 | Shewana3_2659 | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | Lon-A peptidase. Serine peptidase. MEROPS family S16; 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. | 0.699 |
ABK48671.1 | ABK47834.1 | Shewana3_2442 | Shewana3_1600 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | 0.562 |
ABK48671.1 | dnaJ | Shewana3_2442 | Shewana3_0960 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | 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 [...] | 0.670 |
ABK48671.1 | groL | Shewana3_2442 | Shewana3_3567 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.661 |
ABK48671.1 | groS | Shewana3_2442 | Shewana3_3568 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.591 |
ABK48671.1 | grpE | Shewana3_2442 | Shewana3_2902 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like 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 [...] | 0.817 |
ABK48671.1 | hslU | Shewana3_2442 | Shewana3_3700 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like 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. | 0.832 |
ABK48671.1 | hslV | Shewana3_2442 | Shewana3_3699 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | HslV component of HslUV peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.871 |
ABK48671.1 | htpG | Shewana3_2442 | Shewana3_2443 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.905 |
ABK48671.1 | lon | Shewana3_2442 | Shewana3_2659 | PFAM: Thioredoxin domain; KEGG: son:SO2017 putative thioredoxin-like protein. | Lon-A peptidase. Serine peptidase. MEROPS family S16; 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. | 0.537 |
clpP | ABK47834.1 | Shewana3_2661 | Shewana3_1600 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | PFAM: heat shock protein DnaJ domain protein; KEGG: son:SO1850 DnaJ domain protein. | 0.502 |
clpP | dnaJ | Shewana3_2661 | Shewana3_0960 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.516 |