node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dksA | fis | Dda3937_00510 | Dda3937_01595 | RNAP-binding protein modulating ppGpp and iNTP regulation; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. | Global DNA-binding transcriptional dual regulator; Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters; Belongs to the transcriptional regulatory Fis family. | 0.424 |
fis | dksA | Dda3937_01595 | Dda3937_00510 | Global DNA-binding transcriptional dual regulator; Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters; Belongs to the transcriptional regulatory Fis family. | RNAP-binding protein modulating ppGpp and iNTP regulation; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. | 0.424 |
fis | topA | Dda3937_01595 | Dda3937_00587 | Global DNA-binding transcriptional dual regulator; Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters; Belongs to the transcriptional regulatory Fis family. | DNA topoisomerase I, omega subunit; 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 re [...] | 0.467 |
gppA | relA | Dda3937_00264 | Dda3937_00195 | Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase; Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. | GTP pyrophosphokinase / Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.955 |
gyrA | gyrB | Dda3937_01774 | Dda3937_01057 | DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.993 |
gyrA | topA | Dda3937_01774 | Dda3937_00587 | DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | DNA topoisomerase I, omega subunit; 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 re [...] | 0.713 |
gyrB | gyrA | Dda3937_01057 | Dda3937_01774 | DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.993 |
gyrB | topA | Dda3937_01057 | Dda3937_00587 | DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | DNA topoisomerase I, omega subunit; 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 re [...] | 0.743 |
pelD | pelE | Dda3937_03372 | Dda3937_03371 | Pectate lyase D; PelE is secreted by the Out secretion system; Protein involved in pectate lyase activity, polysaccharide catabolic process, carbohydrate catabolic process, interaction with host via protein secreted by type II secretion system, metabolism by symbiont of substance in host and pathogenesis. | Pectate lyase pelE; Involved in maceration and soft-rotting of plant tissue. Pectate lyases have been implicated as pathogenicity factors which induce maceration or rotting of plant tissue. PelE is sufficient to induce these effects under laboratory conditions. | 0.901 |
pelE | pelD | Dda3937_03371 | Dda3937_03372 | Pectate lyase pelE; Involved in maceration and soft-rotting of plant tissue. Pectate lyases have been implicated as pathogenicity factors which induce maceration or rotting of plant tissue. PelE is sufficient to induce these effects under laboratory conditions. | Pectate lyase D; PelE is secreted by the Out secretion system; Protein involved in pectate lyase activity, polysaccharide catabolic process, carbohydrate catabolic process, interaction with host via protein secreted by type II secretion system, metabolism by symbiont of substance in host and pathogenesis. | 0.901 |
relA | gppA | Dda3937_00195 | Dda3937_00264 | GTP pyrophosphokinase / Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase; Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. | 0.955 |
relA | topA | Dda3937_00195 | Dda3937_00587 | GTP pyrophosphokinase / Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | DNA topoisomerase I, omega subunit; 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 re [...] | 0.516 |
topA | fis | Dda3937_00587 | Dda3937_01595 | DNA topoisomerase I, omega subunit; 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 re [...] | Global DNA-binding transcriptional dual regulator; Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters; Belongs to the transcriptional regulatory Fis family. | 0.467 |
topA | gyrA | Dda3937_00587 | Dda3937_01774 | DNA topoisomerase I, omega subunit; 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 re [...] | DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.713 |
topA | gyrB | Dda3937_00587 | Dda3937_01057 | DNA topoisomerase I, omega subunit; 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 re [...] | DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.743 |
topA | relA | Dda3937_00587 | Dda3937_00195 | DNA topoisomerase I, omega subunit; 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 re [...] | GTP pyrophosphokinase / Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.516 |