node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OEF96386.1 | OEF96938.1 | BHF71_04335 | BHF71_04205 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.635 |
OEF96386.1 | groL | BHF71_04335 | BHF71_05690 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.701 |
OEF96386.1 | groS | BHF71_04335 | BHF71_05685 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.760 |
OEF96386.1 | grpE | BHF71_04335 | BHF71_04210 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Nucleotide exchange factor 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 [...] | 0.935 |
OEF96386.1 | hslU | BHF71_04335 | BHF71_00350 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | HslU--HslV peptidase ATPase subunit; 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. | 0.680 |
OEF96386.1 | hslV | BHF71_04335 | BHF71_00345 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.569 |
OEF96386.1 | htpG | BHF71_04335 | BHF71_07190 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.832 |
OEF96386.1 | lon | BHF71_04335 | BHF71_06910 | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Endopeptidase La; 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. | 0.780 |
OEF96938.1 | OEF96386.1 | BHF71_04205 | BHF71_04335 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.635 |
OEF96938.1 | groS | BHF71_04205 | BHF71_05685 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.981 |
OEF96938.1 | grpE | BHF71_04205 | BHF71_04210 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor 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 [...] | 0.977 |
OEF96938.1 | hslU | BHF71_04205 | BHF71_00350 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; 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. | 0.726 |
OEF96938.1 | hslV | BHF71_04205 | BHF71_00345 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.654 |
OEF96938.1 | htpG | BHF71_04205 | BHF71_07190 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.847 |
OEF96938.1 | lon | BHF71_04205 | BHF71_06910 | Chaperonin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Endopeptidase La; 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. | 0.629 |
codY | hslU | BHF71_00355 | BHF71_00350 | Transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | HslU--HslV peptidase ATPase subunit; 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. | 0.940 |
codY | hslV | BHF71_00355 | BHF71_00345 | Transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.786 |
codY | xerC | BHF71_00355 | BHF71_00340 | Transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | Tyrosine recombinase XerD; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.584 |
groL | OEF96386.1 | BHF71_05690 | BHF71_04335 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.701 |
groL | groS | BHF71_05690 | BHF71_05685 | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |