node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SER06328.1 | codY | SAMN04487944_10197 | SAMN04487944_10192 | Flagellar motor switch protein FliG. | Transcriptional pleiotropic repressor; 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. | 0.424 |
SER06328.1 | hslU | SAMN04487944_10197 | SAMN04487944_10191 | Flagellar motor switch protein FliG. | ATP-dependent HslUV 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. | 0.411 |
SER06328.1 | hslV | SAMN04487944_10197 | SAMN04487944_10190 | Flagellar motor switch protein FliG. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.784 |
SES22785.1 | grpE | SAMN04487944_12523 | SAMN04487944_101536 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | Molecular 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 [...] | 0.560 |
SES22785.1 | hslU | SAMN04487944_12523 | SAMN04487944_10191 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | ATP-dependent HslUV 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. | 0.570 |
SES22785.1 | hslV | SAMN04487944_12523 | SAMN04487944_10190 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.741 |
SES22785.1 | htpG | SAMN04487944_12523 | SAMN04487944_11489 | Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.449 |
codY | SER06328.1 | SAMN04487944_10192 | SAMN04487944_10197 | Transcriptional pleiotropic repressor; 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. | Flagellar motor switch protein FliG. | 0.424 |
codY | hslU | SAMN04487944_10192 | SAMN04487944_10191 | Transcriptional pleiotropic repressor; 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. | ATP-dependent HslUV 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. | 0.837 |
codY | hslV | SAMN04487944_10192 | SAMN04487944_10190 | Transcriptional pleiotropic repressor; 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. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.789 |
codY | xerC | SAMN04487944_10192 | SAMN04487944_10189 | Transcriptional pleiotropic repressor; 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. | Integrase/recombinase XerC; 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. | 0.697 |
groL | groS | SAMN04487944_12629 | SAMN04487944_12630 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.999 |
groL | grpE | SAMN04487944_12629 | SAMN04487944_101536 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular 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 [...] | 0.995 |
groL | hslU | SAMN04487944_12629 | SAMN04487944_10191 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent HslUV 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. | 0.827 |
groL | hslV | SAMN04487944_12629 | SAMN04487944_10190 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.828 |
groL | htpG | SAMN04487944_12629 | SAMN04487944_11489 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.935 |
groL | lon | SAMN04487944_12629 | SAMN04487944_109118 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent Lon protease; 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. | 0.832 |
groS | groL | SAMN04487944_12630 | SAMN04487944_12629 | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
groS | grpE | SAMN04487944_12630 | SAMN04487944_101536 | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Molecular 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 [...] | 0.975 |
groS | hslU | SAMN04487944_12630 | SAMN04487944_10191 | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | ATP-dependent HslUV 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. | 0.825 |