| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ping_0841 | Ping_1859 | Ping_0841 | Ping_1859 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.772 |
| Ping_0841 | grpE | Ping_0841 | Ping_0916 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | Co-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-depend [...] | 0.458 |
| Ping_0841 | hslU | Ping_0841 | Ping_0003 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | Heat shock protein HslVU, ATPase 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 |
| Ping_0841 | htpX | Ping_0841 | Ping_1916 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.540 |
| Ping_1859 | Ping_0841 | Ping_1859 | Ping_0841 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | 0.772 |
| Ping_1859 | dnaJ | Ping_1859 | Ping_0918 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 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 between DnaJ, D [...] | 0.764 |
| Ping_1859 | grpE | Ping_1859 | Ping_0916 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Co-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-depend [...] | 0.891 |
| Ping_1859 | hslU | Ping_1859 | Ping_0003 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Heat shock protein HslVU, ATPase 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. | 0.883 |
| Ping_1859 | htpX | Ping_1859 | Ping_1916 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.549 |
| Ping_1914 | Ping_1915 | Ping_1914 | Ping_1915 | PFAM: protein of unknown function DUF490; KEGG: ppr:PBPRA0380 hypothetical protein. | PFAM: surface antigen (D15); KEGG: pat:Patl_0260 surface antigen (D15). | 0.999 |
| Ping_1914 | htpX | Ping_1914 | Ping_1916 | PFAM: protein of unknown function DUF490; KEGG: ppr:PBPRA0380 hypothetical protein. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.494 |
| Ping_1915 | Ping_1914 | Ping_1915 | Ping_1914 | PFAM: surface antigen (D15); KEGG: pat:Patl_0260 surface antigen (D15). | PFAM: protein of unknown function DUF490; KEGG: ppr:PBPRA0380 hypothetical protein. | 0.999 |
| Ping_1915 | htpX | Ping_1915 | Ping_1916 | PFAM: surface antigen (D15); KEGG: pat:Patl_0260 surface antigen (D15). | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.425 |
| Ping_1917 | htpX | Ping_1917 | Ping_1916 | PFAM: PpiC-type peptidyl-prolyl cis-trans isomerase; KEGG: pha:PSHAa2488 peptidyl-prolyl cis-trans isomerase C (rotamase C). | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.517 |
| Ping_2200 | htpX | Ping_2200 | Ping_1916 | Integral inner membrane protein UPF0005; PFAM: protein of unknown function UPF0005; KEGG: cps:CPS_2350 putative membrane protein; Belongs to the BI1 family. | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.599 |
| dnaJ | Ping_1859 | Ping_0918 | Ping_1859 | 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 between DnaJ, D [...] | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.764 |
| dnaJ | ftsH | Ping_0918 | Ping_0811 | 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 between DnaJ, D [...] | Membrane protease FtsH catalytic subunit; 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. | 0.784 |
| dnaJ | grpE | Ping_0918 | Ping_0916 | 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 between DnaJ, D [...] | Co-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-depend [...] | 0.993 |
| dnaJ | hslU | Ping_0918 | Ping_0003 | 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 between DnaJ, D [...] | Heat shock protein HslVU, ATPase 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. | 0.956 |
| dnaJ | htpX | Ping_0918 | Ping_1916 | 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 between DnaJ, D [...] | Heat shock protein, Metallo peptidase, MEROPS family M48B; PFAM: peptidase M48, Ste24p; HtpX domain protein; KEGG: pha:PSHAa1605 heat shock protein; Belongs to the peptidase M48B family. | 0.413 |