| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpE | clpP | LBA0638 | LBA0694 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.947 |
| clpE | groL | LBA0638 | LBA0406 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.887 |
| clpE | grpE | LBA0638 | LBA1248 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | Cochaperonin, Hsp70 cofactor; 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 [...] | 0.831 |
| clpE | hslO | LBA0638 | LBA0279 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | Heat-shock 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. | 0.495 |
| clpE | hslU | LBA0638 | LBA0985 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | ATP dependant protease, ATP binding unit, heatshock protein; 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. | 0.827 |
| clpE | hslV | LBA0638 | LBA0984 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent heat shock protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.803 |
| clpE | topA | LBA0638 | LBA0981 | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.413 |
| clpE-2 | clpP | LBA1910 | LBA0694 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.947 |
| clpE-2 | groL | LBA1910 | LBA0406 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.854 |
| clpE-2 | grpE | LBA1910 | LBA1248 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | Cochaperonin, Hsp70 cofactor; 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 [...] | 0.783 |
| clpE-2 | hslO | LBA1910 | LBA0279 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | Heat-shock 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. | 0.524 |
| clpE-2 | hslU | LBA1910 | LBA0985 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | ATP dependant protease, ATP binding unit, heatshock protein; 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. | 0.788 |
| clpE-2 | hslV | LBA1910 | LBA0984 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | ATP-dependent heat shock protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.771 |
| clpE-2 | topA | LBA1910 | LBA0981 | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.413 |
| clpP | clpE | LBA0694 | LBA0638 | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent Clp protease, ATP-binding subunit; ClpE; Belongs to the ClpA/ClpB family. | 0.947 |
| clpP | clpE-2 | LBA0694 | LBA1910 | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent protease; ClpE; Belongs to the ClpA/ClpB family. | 0.947 |
| clpP | groL | LBA0694 | LBA0406 | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.974 |
| clpP | grpE | LBA0694 | LBA1248 | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Cochaperonin, Hsp70 cofactor; 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 [...] | 0.894 |
| clpP | hslO | LBA0694 | LBA0279 | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Heat-shock 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. | 0.560 |
| clpP | hslU | LBA0694 | LBA0985 | ATP-dependent Clp protease P; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP dependant protease, ATP binding unit, heatshock protein; 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. | 0.728 |