node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ClpP | DnaK | TTE0625 | TTE0955 | Protease subunit of ATP-dependent Clp proteases; 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. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.864 |
ClpP | FliG | TTE0625 | TTE1441 | Protease subunit of ATP-dependent Clp proteases; 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. | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | 0.446 |
ClpP | GroL | TTE0625 | TTE0580 | Protease subunit of ATP-dependent Clp proteases; 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 GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.815 |
ClpP | GrpE | TTE0625 | TTE0954 | Protease subunit of ATP-dependent Clp proteases; 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. | Molecular chaperone GrpE (heat shock 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. [...] | 0.821 |
ClpP | HslV | TTE0625 | TTE1448 | Protease subunit of ATP-dependent Clp proteases; 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. | Proteasome protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.778 |
ClpP | Lon | TTE0625 | TTE0627 | Protease subunit of ATP-dependent Clp proteases; 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 Lon protease, bacterial type; 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. | 0.917 |
DnaK | ClpP | TTE0955 | TTE0625 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Protease subunit of ATP-dependent Clp proteases; 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. | 0.864 |
DnaK | GroL | TTE0955 | TTE0580 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.993 |
DnaK | GrpE | TTE0955 | TTE0954 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperone GrpE (heat shock 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. [...] | 0.999 |
DnaK | HslU | TTE0955 | TTE1447 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent protease, 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. | 0.556 |
DnaK | HslV | TTE0955 | TTE1448 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Proteasome protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.754 |
DnaK | Lon | TTE0955 | TTE0627 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent Lon protease, bacterial type; 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. | 0.717 |
DnaK | TopA | TTE0955 | TTE1449 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Topoisomerase IA; 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 superco [...] | 0.452 |
FliG | ClpP | TTE1441 | TTE0625 | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | Protease subunit of ATP-dependent Clp proteases; 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. | 0.446 |
FliG | HslU | TTE1441 | TTE1447 | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | ATP-dependent protease, 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. | 0.536 |
FliG | HslV | TTE1441 | TTE1448 | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | Proteasome protease subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.774 |
FliG | Smf | TTE1441 | TTE1450 | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | Predicted Rossmann-fold nucleotide-binding protein involved in DNA uptake; Best Blastp hit = gi|7462370|pir||C72399 DNA processing chain A - Thermotoga maritima (strain MSB8) gi|4980749|gb|AAD35341.1|AE001708_9 (AE001708) DNA processing chain A [Thermotoga maritima], score 211, E-value 2.00E-53. | 0.608 |
FliG | TopA | TTE1441 | TTE1449 | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | Topoisomerase IA; 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 superco [...] | 0.580 |
FliG | codY | TTE1441 | TTE1446 | Flagellar motor switch protein; Best Blastp hit = gi|10175077|dbj|BAB06176.1| (AP001515) flagellar motor switch protein [Bacillus halodurans], score 454, E-value 1.00E-127. | 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. | 0.601 |
GroL | ClpP | TTE0580 | TTE0625 | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Protease subunit of ATP-dependent Clp proteases; 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. | 0.815 |