| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ping_0840 | Ping_0841 | Ping_0840 | Ping_0841 | PFAM: major facilitator superfamily MFS_1; KEGG: yps:YPTB2866 putative MFS family 3-phenylpropionic acid transporter. | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | 0.471 |
| Ping_0841 | Ping_0840 | Ping_0841 | Ping_0840 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | PFAM: major facilitator superfamily MFS_1; KEGG: yps:YPTB2866 putative MFS family 3-phenylpropionic acid transporter. | 0.471 |
| Ping_0841 | Ping_0842 | Ping_0841 | Ping_0842 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | KEGG: ppr:PBPRA0377 hypothetical protein. | 0.445 |
| 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. | 0.714 |
| 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 [...] | 0.442 |
| 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. | 0.517 |
| Ping_0841 | hslV | Ping_0841 | Ping_0004 | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.714 |
| Ping_0842 | Ping_0841 | Ping_0842 | Ping_0841 | KEGG: ppr:PBPRA0377 hypothetical protein. | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | 0.445 |
| 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. | 0.714 |
| 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 [...] | 0.783 |
| 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. | 0.797 |
| Ping_1859 | hslV | Ping_1859 | Ping_0004 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.795 |
| grpE | Ping_0841 | Ping_0916 | Ping_0841 | 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 [...] | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | 0.442 |
| grpE | Ping_1859 | Ping_0916 | Ping_1859 | 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 [...] | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.783 |
| grpE | hslU | Ping_0916 | Ping_0003 | 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 [...] | 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. | 0.889 |
| grpE | hslV | Ping_0916 | Ping_0004 | 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 [...] | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.865 |
| hslU | Ping_0841 | Ping_0003 | Ping_0841 | 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. | PFAM: FxsA cytoplasmic membrane protein; KEGG: vpa:VP2862 FxsA protein. | 0.517 |
| hslU | Ping_1859 | Ping_0003 | Ping_1859 | 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. | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.797 |
| hslU | grpE | Ping_0003 | Ping_0916 | 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. | 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 [...] | 0.889 |
| hslU | hslV | Ping_0003 | Ping_0004 | 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. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |