| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AOD14329.1 | AOD14332.1 | BER92_05780 | BER92_05795 | Heat-shock protein 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; Belongs to the HSP33 family. | Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.607 |
| AOD14329.1 | AOD16518.1 | BER92_05780 | BER92_05950 | Heat-shock protein 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; Belongs to the HSP33 family. | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 0.906 |
| AOD14329.1 | dnaJ | BER92_05780 | BER92_07975 | Heat-shock protein 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; Belongs to the HSP33 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, [...] | 0.650 |
| AOD14329.1 | dnaK | BER92_05780 | BER92_07970 | Heat-shock protein 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; Belongs to the HSP33 family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.561 |
| AOD14329.1 | grpE | BER92_05780 | BER92_07965 | Heat-shock protein 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; Belongs to the HSP33 family. | 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 [...] | 0.604 |
| AOD14329.1 | gtrB | BER92_05780 | BER92_05790 | Heat-shock protein 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; Belongs to the HSP33 family. | Glycosyl transferase family 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.578 |
| AOD14329.1 | hslU | BER92_05780 | BER92_02690 | Heat-shock protein 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; Belongs to the HSP33 family. | 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. | 0.715 |
| AOD14329.1 | hslV | BER92_05780 | BER92_02685 | Heat-shock protein 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; Belongs to the HSP33 family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.702 |
| AOD14329.1 | lon | BER92_05780 | BER92_14370 | Heat-shock protein 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; Belongs to the HSP33 family. | 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. | 0.606 |
| AOD14329.1 | mtgA | BER92_05780 | BER92_05785 | Heat-shock protein 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; Belongs to the HSP33 family. | Monofunctional biosynthetic peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.712 |
| AOD14332.1 | AOD14329.1 | BER92_05795 | BER92_05780 | Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein 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; Belongs to the HSP33 family. | 0.607 |
| AOD14332.1 | gtrB | BER92_05795 | BER92_05790 | Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Glycosyl transferase family 2; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.803 |
| AOD14332.1 | mtgA | BER92_05795 | BER92_05785 | Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Monofunctional biosynthetic peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. | 0.834 |
| AOD16518.1 | AOD14329.1 | BER92_05950 | BER92_05780 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Heat-shock protein 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; Belongs to the HSP33 family. | 0.906 |
| AOD16518.1 | dnaJ | BER92_05950 | BER92_07975 | RNA-binding 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, [...] | 0.636 |
| AOD16518.1 | grpE | BER92_05950 | BER92_07965 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 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 [...] | 0.636 |
| AOD16518.1 | hslU | BER92_05950 | BER92_02690 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 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. | 0.678 |
| AOD16518.1 | hslV | BER92_05950 | BER92_02685 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.712 |
| dnaJ | AOD14329.1 | BER92_07975 | BER92_05780 | 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 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; Belongs to the HSP33 family. | 0.650 |
| dnaJ | AOD16518.1 | BER92_07975 | BER92_05950 | 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, [...] | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 0.636 |
