node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Gura_1521 | clpB | Gura_1521 | Gura_3955 | Molecular chaperone-like protein. | ATPase AAA-2 domain protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.968 |
Gura_1521 | clpP | Gura_1521 | Gura_1915 | Molecular chaperone-like protein. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.688 |
Gura_1521 | dnaJ | Gura_1521 | Gura_0212 | Molecular chaperone-like protein. | 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 [...] | 0.935 |
Gura_1521 | groL | Gura_1521 | Gura_4307 | Molecular chaperone-like protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.936 |
Gura_1521 | groS | Gura_1521 | Gura_4306 | Molecular chaperone-like protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.890 |
Gura_1521 | grpE | Gura_1521 | Gura_0210 | Molecular chaperone-like protein. | 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 [...] | 0.976 |
Gura_1521 | htpG | Gura_1521 | Gura_1728 | Molecular chaperone-like protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.984 |
Gura_1521 | lon | Gura_1521 | Gura_0691 | Molecular chaperone-like protein. | 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. | 0.530 |
Gura_2824 | clpB | Gura_2824 | Gura_3955 | 2-alkenal reductase; PFAM: Heat shock protein 70. | ATPase AAA-2 domain protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.983 |
Gura_2824 | clpP | Gura_2824 | Gura_1915 | 2-alkenal reductase; PFAM: Heat shock protein 70. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.746 |
Gura_2824 | dnaJ | Gura_2824 | Gura_0212 | 2-alkenal reductase; PFAM: Heat shock protein 70. | 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 [...] | 0.997 |
Gura_2824 | groL | Gura_2824 | Gura_4307 | 2-alkenal reductase; PFAM: Heat shock protein 70. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.961 |
Gura_2824 | groS | Gura_2824 | Gura_4306 | 2-alkenal reductase; PFAM: Heat shock protein 70. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.920 |
Gura_2824 | grpE | Gura_2824 | Gura_0210 | 2-alkenal reductase; PFAM: Heat shock protein 70. | 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 [...] | 0.992 |
Gura_2824 | htpG | Gura_2824 | Gura_1728 | 2-alkenal reductase; PFAM: Heat shock protein 70. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.988 |
Gura_2824 | lon | Gura_2824 | Gura_0691 | 2-alkenal reductase; PFAM: Heat shock protein 70. | 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. | 0.600 |
clpB | Gura_1521 | Gura_3955 | Gura_1521 | ATPase AAA-2 domain protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Molecular chaperone-like protein. | 0.968 |
clpB | Gura_2824 | Gura_3955 | Gura_2824 | ATPase AAA-2 domain protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 2-alkenal reductase; PFAM: Heat shock protein 70. | 0.983 |
clpB | clpP | Gura_3955 | Gura_1915 | ATPase AAA-2 domain protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.976 |
clpB | dnaJ | Gura_3955 | Gura_0212 | ATPase AAA-2 domain protein; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB 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 [...] | 0.884 |