node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Pden_1373 | Pden_2371 | Pden_1373 | Pden_2371 | KEGG: rde:RD1_4059 Lon protease, putative. | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | 0.432 |
Pden_1373 | Pden_2573 | Pden_1373 | Pden_2573 | KEGG: rde:RD1_4059 Lon protease, putative. | Hsp33 protein; 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. | 0.454 |
Pden_1373 | clpX | Pden_1373 | Pden_1266 | KEGG: rde:RD1_4059 Lon protease, putative. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.568 |
Pden_1373 | dnaJ | Pden_1373 | Pden_2303 | KEGG: rde:RD1_4059 Lon protease, putative. | 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 [...] | 0.744 |
Pden_1373 | dnaK | Pden_1373 | Pden_2302 | KEGG: rde:RD1_4059 Lon protease, putative. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.686 |
Pden_1373 | groL1 | Pden_1373 | Pden_3654 | KEGG: rde:RD1_4059 Lon protease, putative. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.740 |
Pden_1373 | grpE | Pden_1373 | Pden_0008 | KEGG: rde:RD1_4059 Lon protease, putative. | GrpE protein; 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-dependent i [...] | 0.720 |
Pden_1373 | hslU | Pden_1373 | Pden_2790 | KEGG: rde:RD1_4059 Lon protease, putative. | 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. | 0.744 |
Pden_1373 | hslV | Pden_1373 | Pden_2791 | KEGG: rde:RD1_4059 Lon protease, putative. | 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. | 0.719 |
Pden_2371 | Pden_1373 | Pden_2371 | Pden_1373 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | KEGG: rde:RD1_4059 Lon protease, putative. | 0.432 |
Pden_2371 | Pden_2573 | Pden_2371 | Pden_2573 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | Hsp33 protein; 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. | 0.445 |
Pden_2371 | dnaJ | Pden_2371 | Pden_2303 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | 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 [...] | 0.737 |
Pden_2371 | dnaK | Pden_2371 | Pden_2302 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.607 |
Pden_2371 | groL1 | Pden_2371 | Pden_3654 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.654 |
Pden_2371 | grpE | Pden_2371 | Pden_0008 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | GrpE protein; 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-dependent i [...] | 0.831 |
Pden_2371 | hslU | Pden_2371 | Pden_2790 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | 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. | 0.844 |
Pden_2371 | hslV | Pden_2371 | Pden_2791 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | 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. | 0.832 |
Pden_2371 | lon | Pden_2371 | Pden_3609 | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | ATP-dependent proteinase, Serine peptidase, MEROPS family S16; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.432 |
Pden_2573 | Pden_1373 | Pden_2573 | Pden_1373 | Hsp33 protein; 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. | KEGG: rde:RD1_4059 Lon protease, putative. | 0.454 |
Pden_2573 | Pden_2371 | Pden_2573 | Pden_2371 | Hsp33 protein; 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. | PFAM: Thioredoxin domain; KEGG: rsp:RSP_1489 protein containing thioredoxin domain. | 0.445 |