| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KIC57016.1 | KIC58846.1 | RM53_10515 | RM53_06450 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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; Belongs to the HSP33 family. | 0.417 |
| KIC57016.1 | KIC59662.1 | RM53_10515 | RM53_04355 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.404 |
| KIC57016.1 | dnaJ | RM53_10515 | RM53_10785 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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, [...] | 0.751 |
| KIC57016.1 | dnaK | RM53_10515 | RM53_10790 | Thioredoxin; 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. | 0.627 |
| KIC57016.1 | groEL | RM53_10515 | RM53_08060 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.735 |
| KIC57016.1 | groS | RM53_10515 | RM53_08055 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.618 |
| KIC57016.1 | grpE | RM53_10515 | RM53_00895 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock 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- [...] | 0.833 |
| KIC57016.1 | hslU | RM53_10515 | RM53_09405 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; 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. | 0.869 |
| KIC57016.1 | hslV | RM53_10515 | RM53_01610 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.856 |
| KIC57016.1 | lon | RM53_10515 | RM53_12920 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.621 |
| KIC58846.1 | KIC57016.1 | RM53_06450 | RM53_10515 | 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; Belongs to the HSP33 family. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.417 |
| KIC58846.1 | dnaJ | RM53_06450 | RM53_10785 | 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; 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, [...] | 0.611 |
| KIC58846.1 | groEL | RM53_06450 | RM53_08060 | 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; Belongs to the HSP33 family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.448 |
| KIC58846.1 | grpE | RM53_06450 | RM53_00895 | 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; Belongs to the HSP33 family. | Heat shock 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- [...] | 0.601 |
| KIC58846.1 | hslU | RM53_06450 | RM53_09405 | 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; Belongs to the HSP33 family. | ATP-dependent protease; 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. | 0.749 |
| KIC58846.1 | hslV | RM53_06450 | RM53_01610 | 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; Belongs to the HSP33 family. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.700 |
| KIC58846.1 | lon | RM53_06450 | RM53_12920 | 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; Belongs to the HSP33 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. | 0.643 |
| KIC59662.1 | KIC57016.1 | RM53_04355 | RM53_10515 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.404 |
| KIC59662.1 | dnaK | RM53_04355 | RM53_10790 | Molecular chaperone DnaJ; 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. | 0.997 |
| KIC59662.1 | groEL | RM53_04355 | RM53_08060 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.830 |
STRING v12.5 is now available!
