| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RSc1132 | RSc1133 | RSc1132 | RSc1133 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Putative carbonic anhydrase/acetyltransferase protein. | 0.806 |
| RSc1132 | RSc1134 | RSc1132 | RSc1134 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | 0.597 |
| RSc1132 | RSc1602 | RSc1132 | RSc1602 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Putative peptidase t1a, proteasome beta-subunit; protein. | 0.803 |
| RSc1132 | dnaJ | RSc1132 | RSc2634 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Probable 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 betwee [...] | 0.683 |
| RSc1132 | grpE | RSc1132 | RSc2639 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Probable protein grpe (hsp-70 cofactor); 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. Severa [...] | 0.622 |
| RSc1132 | hslR | RSc1132 | RSc2642 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Putative heat shock protein 15. | 0.892 |
| RSc1132 | hslU | RSc1132 | RSc0042 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Probable atp-dependent hsl protease atp-binding subunit hslu protein; 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. | 0.726 |
| RSc1132 | hslV | RSc1132 | RSc0043 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Probable atp-dependent protease hslv protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.625 |
| RSc1132 | lon | RSc1132 | RSc1713 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Probable atp-dependent protease la 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. | 0.614 |
| RSc1132 | mopA | RSc1132 | RSc0642 | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | Probable 60 kda chaperonin (protein cpn60) (groel protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.601 |
| RSc1133 | RSc1132 | RSc1133 | RSc1132 | Putative carbonic anhydrase/acetyltransferase protein. | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | 0.806 |
| RSc1133 | RSc1134 | RSc1133 | RSc1134 | Putative carbonic anhydrase/acetyltransferase protein. | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | 0.597 |
| RSc1134 | RSc1132 | RSc1134 | RSc1132 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | 0.597 |
| RSc1134 | RSc1133 | RSc1134 | RSc1133 | Conserved hypothetical protein; Miscellaneous; hypothetical/global homology. | Putative carbonic anhydrase/acetyltransferase protein. | 0.597 |
| RSc1602 | RSc1132 | RSc1602 | RSc1132 | Putative peptidase t1a, proteasome beta-subunit; protein. | Putative redox regulated molecular chaperone heat-shock-like 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; Belongs to the HSP33 family. | 0.803 |
| RSc1602 | dnaJ | RSc1602 | RSc2634 | Putative peptidase t1a, proteasome beta-subunit; protein. | Probable 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 betwee [...] | 0.584 |
| RSc1602 | grpE | RSc1602 | RSc2639 | Putative peptidase t1a, proteasome beta-subunit; protein. | Probable protein grpe (hsp-70 cofactor); 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. Severa [...] | 0.735 |
| RSc1602 | hslR | RSc1602 | RSc2642 | Putative peptidase t1a, proteasome beta-subunit; protein. | Putative heat shock protein 15. | 0.623 |
| RSc1602 | hslU | RSc1602 | RSc0042 | Putative peptidase t1a, proteasome beta-subunit; protein. | Probable atp-dependent hsl protease atp-binding subunit hslu protein; 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. | 0.957 |
| RSc1602 | lon | RSc1602 | RSc1713 | Putative peptidase t1a, proteasome beta-subunit; protein. | Probable atp-dependent protease la 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. | 0.709 |