| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SPO0023 | SPO0025 | SPO0023 | SPO0025 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293; Belongs to the Nudix hydrolase family. | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293. | 0.594 |
| SPO0023 | SPO0026 | SPO0023 | SPO0026 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293; Belongs to the Nudix hydrolase family. | Identified by match to protein family HMM PF01743; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | 0.694 |
| SPO0023 | hslO | SPO0023 | SPO0024 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293; Belongs to the Nudix hydrolase family. | Chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.705 |
| SPO0023 | rumA | SPO0023 | SPO0029 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293; Belongs to the Nudix hydrolase family. | 23S rRNA (Uracil-5-)-methyltransferase rumA; Identified by similarity to SP:P55135; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. | 0.445 |
| SPO0025 | SPO0023 | SPO0025 | SPO0023 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293. | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293; Belongs to the Nudix hydrolase family. | 0.594 |
| SPO0025 | SPO0026 | SPO0025 | SPO0026 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293. | Identified by match to protein family HMM PF01743; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | 0.827 |
| SPO0025 | hslO | SPO0025 | SPO0024 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293. | Chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.808 |
| SPO0025 | rumA | SPO0025 | SPO0029 | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293. | 23S rRNA (Uracil-5-)-methyltransferase rumA; Identified by similarity to SP:P55135; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. | 0.462 |
| SPO0026 | SPO0023 | SPO0026 | SPO0023 | Identified by match to protein family HMM PF01743; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293; Belongs to the Nudix hydrolase family. | 0.694 |
| SPO0026 | SPO0025 | SPO0026 | SPO0025 | Identified by match to protein family HMM PF01743; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | Hydrolase, NUDIX family; Identified by match to protein family HMM PF00293. | 0.827 |
| SPO0026 | hslO | SPO0026 | SPO0024 | Identified by match to protein family HMM PF01743; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | Chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.843 |
| SPO0026 | rumA | SPO0026 | SPO0029 | Identified by match to protein family HMM PF01743; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. | 23S rRNA (Uracil-5-)-methyltransferase rumA; Identified by similarity to SP:P55135; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. | 0.663 |
| SPO1418 | grpE | SPO1418 | SPO0010 | S4 domain protein; Identified by match to protein family HMM PF01479. | 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 [...] | 0.589 |
| SPO1418 | hslO | SPO1418 | SPO0024 | S4 domain protein; Identified by match to protein family HMM PF01479. | Chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.863 |
| SPO1418 | hslU | SPO1418 | SPO3882 | S4 domain protein; Identified by match to protein family HMM PF01479. | ATP-dependent hsl protease, ATP-binding 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. | 0.675 |
| SPO1418 | hslV | SPO1418 | SPO3880 | S4 domain protein; Identified by match to protein family HMM PF01479. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.776 |
| groEL | grpE | SPO0887 | SPO0010 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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 [...] | 0.983 |
| groEL | hslO | SPO0887 | SPO0024 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.560 |
| groEL | hslU | SPO0887 | SPO3882 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent hsl protease, ATP-binding 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. | 0.896 |
| groEL | hslV | SPO0887 | SPO3880 | Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.887 |