| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa0261 | PSHAa2342 | PSHAa0261 | PSHAa2342 | Putative FxsA protein (Suppressor of F exclusion of phage T7); Function of homologous gene experimentally demonstrated in an other organism; membrane component. | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.830 |
| PSHAa0261 | grpE | PSHAa0261 | PSHAa1222 | Putative FxsA protein (Suppressor of F exclusion of phage T7); Function of homologous gene experimentally demonstrated in an other organism; membrane component. | 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 [...] | 0.405 |
| PSHAa0261 | hslU | PSHAa0261 | PSHAa2731 | Putative FxsA protein (Suppressor of F exclusion of phage T7); Function of homologous gene experimentally demonstrated in an other organism; membrane component. | 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. | 0.558 |
| PSHAa0261 | htpX | PSHAa0261 | PSHAa1605 | Putative FxsA protein (Suppressor of F exclusion of phage T7); Function of homologous gene experimentally demonstrated in an other organism; membrane component. | Zinc metalloprotease HtpX, membrane-bound with cytosolic active site; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase M48B family. | 0.580 |
| PSHAa0544 | htpX | PSHAa0544 | PSHAa1605 | Putative peptidase, M23/M37 family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; enzyme. | Zinc metalloprotease HtpX, membrane-bound with cytosolic active site; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase M48B family. | 0.606 |
| PSHAa1683 | htpX | PSHAa1683 | PSHAa1605 | Putative transport protein (TEGT family) (partial match); Function of strongly homologous gene; transporter; Belongs to the BI1 family. | Zinc metalloprotease HtpX, membrane-bound with cytosolic active site; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase M48B family. | 0.671 |
| PSHAa2342 | PSHAa0261 | PSHAa2342 | PSHAa0261 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Putative FxsA protein (Suppressor of F exclusion of phage T7); Function of homologous gene experimentally demonstrated in an other organism; membrane component. | 0.830 |
| 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 | ftsH | PSHAa2342 | PSHAa0870 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Cell division protease ftsH, ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.408 |
| 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 | htpX | PSHAa2342 | PSHAa1605 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Zinc metalloprotease HtpX, membrane-bound with cytosolic active site; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase M48B family. | 0.590 |
| bioD | htpX | PSHAa1606 | PSHAa1605 | Desthiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. | Zinc metalloprotease HtpX, membrane-bound with cytosolic active site; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase M48B family. | 0.553 |
| 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 | ftsH | PSHAb0358 | PSHAa0870 | 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 [...] | Cell division protease ftsH, ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.795 |
| 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 | htpX | PSHAb0358 | PSHAa1605 | 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 [...] | Zinc metalloprotease HtpX, membrane-bound with cytosolic active site; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase M48B family. | 0.609 |
| ftsH | PSHAa2342 | PSHAa0870 | PSHAa2342 | Cell division protease ftsH, ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.408 |
| ftsH | dnaJ | PSHAa0870 | PSHAb0358 | Cell division protease ftsH, ATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 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 [...] | 0.795 |