node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
APF04193.1 | dnaK | BIZ52_12870 | BIZ52_09930 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
APF04193.1 | groL | BIZ52_12870 | BIZ52_03755 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.875 |
APF04193.1 | groS | BIZ52_12870 | BIZ52_03750 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.604 |
APF04193.1 | grpE | BIZ52_12870 | BIZ52_09935 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Nucleotide exchange factor 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 [...] | 0.930 |
APF04193.1 | hslU | BIZ52_12870 | BIZ52_03470 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | HslU--HslV peptidase ATPase subunit; 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. | 0.722 |
APF04193.1 | htpG | BIZ52_12870 | BIZ52_06440 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Glucosyltransferase Lgt1; Molecular chaperone. Has ATPase activity. | 0.979 |
APF04193.1 | lon | BIZ52_12870 | BIZ52_08930 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Endopeptidase 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. | 0.598 |
cbpA | dnaK | BIZ52_10795 | BIZ52_09930 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
cbpA | groL | BIZ52_10795 | BIZ52_03755 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.889 |
cbpA | groS | BIZ52_10795 | BIZ52_03750 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.724 |
cbpA | grpE | BIZ52_10795 | BIZ52_09935 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor 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 [...] | 0.969 |
cbpA | hslU | BIZ52_10795 | BIZ52_03470 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; 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. | 0.738 |
cbpA | htpG | BIZ52_10795 | BIZ52_06440 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glucosyltransferase Lgt1; Molecular chaperone. Has ATPase activity. | 0.979 |
cbpA | lon | BIZ52_10795 | BIZ52_08930 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Endopeptidase 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. | 0.598 |
cbpA | rpoH | BIZ52_10795 | BIZ52_13895 | Cytochrome C biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | RNA polymerase factor sigma-32; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.417 |
dnaJ | dnaK | BIZ52_09925 | BIZ52_09930 | 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 DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groL | BIZ52_09925 | BIZ52_03755 | 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, [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.946 |
dnaJ | groS | BIZ52_09925 | BIZ52_03750 | 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, [...] | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.870 |
dnaJ | grpE | BIZ52_09925 | BIZ52_09935 | 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, [...] | Nucleotide exchange factor 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 [...] | 0.985 |
dnaJ | hslU | BIZ52_09925 | BIZ52_03470 | 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, [...] | HslU--HslV peptidase ATPase subunit; 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. | 0.954 |