| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ping_0212 | Ping_1859 | Ping_0212 | Ping_1859 | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.422 |
| Ping_0212 | apaH | Ping_0212 | Ping_1046 | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | Bis(5'nucleosyl)-tetraphosphatase, ApaH; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | 0.455 |
| Ping_0212 | dnaJ | Ping_0212 | Ping_0918 | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 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 [...] | 0.422 |
| Ping_0212 | engB | Ping_0212 | Ping_0211 | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | Cell division checkpoint GTPase YihA; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.417 |
| Ping_0212 | htpG | Ping_0212 | Ping_0956 | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.437 |
| Ping_0212 | rsmJ | Ping_0212 | Ping_2836 | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | Hypothetical protein DUF548; Specifically methylates the guanosine in position 1516 of 16S rRNA. | 0.677 |
| Ping_1859 | Ping_0212 | Ping_1859 | Ping_0212 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 0.422 |
| 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 | htpG | Ping_1859 | Ping_0956 | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.773 |
| apaH | Ping_0212 | Ping_1046 | Ping_0212 | Bis(5'nucleosyl)-tetraphosphatase, ApaH; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family. | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 0.455 |
| dnaJ | Ping_0212 | Ping_0918 | Ping_0212 | 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 [...] | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 0.422 |
| 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 | engB | Ping_0918 | Ping_0211 | 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 [...] | Cell division checkpoint GTPase YihA; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.419 |
| dnaJ | htpG | Ping_0918 | Ping_0956 | 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 Hsp90; Molecular chaperone. Has ATPase activity. | 0.986 |
| engB | Ping_0212 | Ping_0211 | Ping_0212 | Cell division checkpoint GTPase YihA; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 0.417 |
| engB | dnaJ | Ping_0211 | Ping_0918 | Cell division checkpoint GTPase YihA; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 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 [...] | 0.419 |
| htpG | Ping_0212 | Ping_0956 | Ping_0212 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 0.437 |
| htpG | Ping_1859 | Ping_0956 | Ping_1859 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | PFAM: Thioredoxin domain; KEGG: eca:ECA1220 putative thioredoxin. | 0.773 |
| htpG | dnaJ | Ping_0956 | Ping_0918 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 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 [...] | 0.986 |
| rsmJ | Ping_0212 | Ping_2836 | Ping_0212 | Hypothetical protein DUF548; Specifically methylates the guanosine in position 1516 of 16S rRNA. | Oligopeptidase A, Metallo peptidase, MEROPS family M03A; PFAM: peptidase M3A and M3B, thimet/oligopeptidase F; KEGG: shm:Shewmr7_3935 oligopeptidase A. | 0.677 |