| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AOI81578.1 | AOI83008.1 | WI67_03505 | WI67_11405 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hsp33 chaperonin; 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. | 0.865 |
| AOI81578.1 | dnaJ | WI67_03505 | WI67_03525 | RNA-binding protein; 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, [...] | 0.555 |
| AOI81578.1 | grpE | WI67_03505 | WI67_03510 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 [...] | 0.555 |
| AOI81578.1 | hslU | WI67_03505 | WI67_16465 | RNA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.561 |
| AOI81578.1 | hslV | WI67_03505 | WI67_16460 | RNA-binding protein; 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. | 0.769 |
| AOI83006.1 | AOI83007.1 | WI67_11395 | WI67_11400 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Gamma carbonic anhydrase family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.551 |
| AOI83006.1 | AOI83008.1 | WI67_11395 | WI67_11405 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hsp33 chaperonin; 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. | 0.544 |
| AOI83007.1 | AOI83006.1 | WI67_11400 | WI67_11395 | Gamma carbonic anhydrase family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.551 |
| AOI83007.1 | AOI83008.1 | WI67_11400 | WI67_11405 | Gamma carbonic anhydrase family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hsp33 chaperonin; 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. | 0.709 |
| AOI83008.1 | AOI81578.1 | WI67_11405 | WI67_03505 | Hsp33 chaperonin; 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. | 0.865 |
| AOI83008.1 | AOI83006.1 | WI67_11405 | WI67_11395 | Hsp33 chaperonin; 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.544 |
| AOI83008.1 | AOI83007.1 | WI67_11405 | WI67_11400 | Hsp33 chaperonin; 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. | Gamma carbonic anhydrase family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.709 |
| AOI83008.1 | AhpF | WI67_11405 | WI67_22665 | Hsp33 chaperonin; 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. | Alkyl hydroperoxide reductase subunit F; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.543 |
| AOI83008.1 | dnaJ | WI67_11405 | WI67_03525 | Hsp33 chaperonin; 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, [...] | 0.620 |
| AOI83008.1 | dusA | WI67_11405 | WI67_07795 | Hsp33 chaperonin; 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. | tRNA-dihydrouridine synthase A; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. | 0.607 |
| AOI83008.1 | grpE | WI67_11405 | WI67_03510 | Hsp33 chaperonin; 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 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 [...] | 0.563 |
| AOI83008.1 | hslU | WI67_11405 | WI67_16465 | Hsp33 chaperonin; 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 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. | 0.757 |
| AOI83008.1 | hslV | WI67_11405 | WI67_16460 | Hsp33 chaperonin; 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. | 0.646 |
| AOI83008.1 | tig | WI67_11405 | WI67_10220 | Hsp33 chaperonin; 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. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.627 |
| AhpF | AOI83008.1 | WI67_22665 | WI67_11405 | Alkyl hydroperoxide reductase subunit F; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hsp33 chaperonin; 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. | 0.543 |