| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KOO02842.1 | dnaJ | AKJ17_13000 | AKJ17_07795 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Molecular chaperone 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, [...] | 0.575 |
| KOO02842.1 | grpE | AKJ17_13000 | AKJ17_07810 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Heat -hock protein GrpE; 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- [...] | 0.594 |
| KOO02842.1 | hslO | AKJ17_13000 | AKJ17_12995 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Molecular chaperone Hsp33; 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. | 0.956 |
| KOO02842.1 | hslU | AKJ17_13000 | AKJ17_14400 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | ATP-dependent protease ATP-binding 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. | 0.590 |
| KOO02842.1 | hslV | AKJ17_13000 | AKJ17_14395 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.711 |
| KOO02842.1 | htpG | AKJ17_13000 | AKJ17_16570 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.513 |
| KOO02842.1 | lon | AKJ17_13000 | AKJ17_13950 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | DNA-binding protein; 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. | 0.437 |
| KOO03896.1 | hslO | AKJ17_07435 | AKJ17_12995 | ArsC family transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ArsC family. | Molecular chaperone Hsp33; 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. | 0.531 |
| KOO04911.1 | dnaJ | AKJ17_03215 | AKJ17_07795 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | Molecular chaperone 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, [...] | 0.659 |
| KOO04911.1 | grpE | AKJ17_03215 | AKJ17_07810 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | Heat -hock protein GrpE; 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- [...] | 0.709 |
| KOO04911.1 | hslO | AKJ17_03215 | AKJ17_12995 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | Molecular chaperone Hsp33; 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. | 0.541 |
| KOO04911.1 | hslU | AKJ17_03215 | AKJ17_14400 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | ATP-dependent protease ATP-binding 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. | 0.593 |
| KOO04911.1 | hslV | AKJ17_03215 | AKJ17_14395 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.614 |
| KOO04911.1 | htpG | AKJ17_03215 | AKJ17_16570 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.774 |
| KOO04911.1 | lon | AKJ17_03215 | AKJ17_13950 | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | DNA-binding protein; 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. | 0.626 |
| dnaJ | KOO02842.1 | AKJ17_07795 | AKJ17_13000 | Molecular chaperone 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, [...] | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 0.575 |
| dnaJ | KOO04911.1 | AKJ17_07795 | AKJ17_03215 | Molecular chaperone 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, [...] | Heat-shock protein Hsp20; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the small heat shock protein (HSP20) family. | 0.659 |
| dnaJ | groEL | AKJ17_07795 | AKJ17_17305 | Molecular chaperone 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, [...] | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.945 |
| dnaJ | grpE | AKJ17_07795 | AKJ17_07810 | Molecular chaperone 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, [...] | Heat -hock protein GrpE; 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- [...] | 0.979 |
| dnaJ | hslO | AKJ17_07795 | AKJ17_12995 | Molecular chaperone 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, [...] | Molecular chaperone Hsp33; 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. | 0.596 |