node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
bscR | cypB | BSU27170 | BSU27160 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. | 0.994 |
bscR | epsB | BSU27170 | BSU34360 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Protein tyrosine kinase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the CpsD/CapB family. | 0.608 |
bscR | ptkA | BSU27170 | BSU36250 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | 0.912 |
bscR | salA | BSU27170 | BSU01540 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Mrp family regulator; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.634 |
bscR | ssbA | BSU27170 | BSU40900 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Single-strand DNA-binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. Has a 20-fold higher affinity for ssDNA than SsbB; SsbA and DprA activate the homologuos DNA strand exchange function of RecA-ATP. | 0.571 |
bscR | yhcY | BSU27170 | BSU09320 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Two-component sensor histidine kinase [YhcZ]; Member of the two-component regulatory system YhcY/YhcZ. Probably activates YhcZ by phosphorylation. | 0.678 |
bscR | yhcZ | BSU27170 | BSU09330 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Two-component response regulator [YhcY]; Member of the two-component regulatory system YhcY/YhcZ. | 0.634 |
bscR | yobD | BSU27170 | BSU18850 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Transcriptional regulator (phage-related, Xre family); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin. | 0.685 |
bscR | yorK | BSU27170 | BSU20350 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Putative single-strand DNA-specific exonuclease; Putative single-stranded-DNA-specific exonuclease. | 0.752 |
bscR | yrhH | BSU27170 | BSU27180 | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | Putative methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.896 |
cypB | bscR | BSU27160 | BSU27170 | Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | 0.994 |
cypB | ptkA | BSU27160 | BSU36250 | Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | 0.495 |
cypB | yrhH | BSU27160 | BSU27180 | Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. | Putative methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.901 |
epsB | bscR | BSU34360 | BSU27170 | Protein tyrosine kinase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the CpsD/CapB family. | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | 0.608 |
epsB | ptkA | BSU34360 | BSU36250 | Protein tyrosine kinase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the CpsD/CapB family. | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | 0.448 |
ptkA | bscR | BSU36250 | BSU27170 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Transcriptional regulator for cypB; Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon. | 0.912 |
ptkA | cypB | BSU36250 | BSU27160 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. | 0.495 |
ptkA | epsB | BSU36250 | BSU34360 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Protein tyrosine kinase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the CpsD/CapB family. | 0.448 |
ptkA | salA | BSU36250 | BSU01540 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Mrp family regulator; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.857 |
ptkA | ssbA | BSU36250 | BSU40900 | Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family. | Single-strand DNA-binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. Has a 20-fold higher affinity for ssDNA than SsbB; SsbA and DprA activate the homologuos DNA strand exchange function of RecA-ATP. | 0.689 |