| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa2342 | PSHAa2732 | PSHAa2342 | PSHAa2732 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Homologs of previously reported genes of unknown function. | 0.443 |
| PSHAa2342 | dnaJ | PSHAa2342 | PSHAb0358 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | 0.702 |
| PSHAa2342 | dnaK | PSHAa2342 | PSHAb0357 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.473 |
| PSHAa2342 | groL | PSHAa2342 | PSHAa0259 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.908 |
| PSHAa2342 | groS | PSHAa2342 | PSHAa0260 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 10 kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.563 |
| PSHAa2342 | grpE | PSHAa2342 | PSHAa1222 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Hsp 24 DnaK nucleotide exchange factor; 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 [...] | 0.901 |
| PSHAa2342 | hslU | PSHAa2342 | PSHAa2731 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.897 |
| PSHAa2342 | hslV | PSHAa2342 | PSHAa2730 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.915 |
| PSHAa2342 | htpG | PSHAa2342 | PSHAa1207 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.785 |
| PSHAa2342 | lon | PSHAa2342 | PSHAa2060 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | DNA-binding ATP-dependent protease 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. | 0.600 |
| PSHAa2732 | PSHAa2342 | PSHAa2732 | PSHAa2342 | Homologs of previously reported genes of unknown function. | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.443 |
| PSHAa2732 | hslU | PSHAa2732 | PSHAa2731 | Homologs of previously reported genes of unknown function. | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.838 |
| PSHAa2732 | hslV | PSHAa2732 | PSHAa2730 | Homologs of previously reported genes of unknown function. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.849 |
| dnaJ | PSHAa2342 | PSHAb0358 | PSHAa2342 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.702 |
| dnaJ | dnaK | PSHAb0358 | PSHAb0357 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Chaperone protein dnaK (Heat shock protein 70) (Heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | PSHAb0358 | PSHAa0259 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | 60 kDa chaperonin (Protein Cpn60) (groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.990 |
| dnaJ | groS | PSHAb0358 | PSHAa0260 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | 10 kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.966 |
| dnaJ | grpE | PSHAb0358 | PSHAa1222 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Hsp 24 DnaK nucleotide exchange factor; 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 [...] | 0.994 |
| dnaJ | hslU | PSHAb0358 | PSHAa2731 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | ATPase component of the HslUV protease, also functions as molecular chaperone; 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. | 0.961 |
| dnaJ | hslV | PSHAb0358 | PSHAa2730 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.932 |
