| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cdsA | dxr | BSU16540 | BSU16550 | Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. | 0.924 |
| cdsA | proS | BSU16540 | BSU16570 | Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.723 |
| cdsA | rseP | BSU16540 | BSU16560 | Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.855 |
| cdsA | uppS | BSU16540 | BSU16530 | Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Undecaprenyl pyrophosphate synthase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | 0.998 |
| dxr | cdsA | BSU16550 | BSU16540 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. | Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.924 |
| dxr | proS | BSU16550 | BSU16570 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.827 |
| dxr | rseP | BSU16550 | BSU16560 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.937 |
| dxr | uppS | BSU16550 | BSU16530 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. | Undecaprenyl pyrophosphate synthase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | 0.973 |
| ecsA | rseP | BSU10040 | BSU16560 | ABC transporter (ATP-binding protein); Has a role in exoprotein production, sporulation and competence. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.918 |
| ecsA | rsiW | BSU10040 | BSU01740 | ABC transporter (ATP-binding protein); Has a role in exoprotein production, sporulation and competence. | anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...] | 0.680 |
| ecsA | uppS | BSU10040 | BSU16530 | ABC transporter (ATP-binding protein); Has a role in exoprotein production, sporulation and competence. | Undecaprenyl pyrophosphate synthase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | 0.408 |
| htpX | prsW | BSU13490 | BSU22940 | Membrane protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the peptidase M48B family. | Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...] | 0.634 |
| htpX | rseP | BSU13490 | BSU16560 | Membrane protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the peptidase M48B family. | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.861 |
| proS | cdsA | BSU16570 | BSU16540 | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | Phosphatidate cytidylyltransferase (CDP-diglyceride synthase); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.723 |
| proS | dxr | BSU16570 | BSU16550 | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family. | 0.827 |
| proS | rseP | BSU16570 | BSU16560 | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.843 |
| proS | uppS | BSU16570 | BSU16530 | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | Undecaprenyl pyrophosphate synthase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. | 0.915 |
| prsW | htpX | BSU22940 | BSU13490 | Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...] | Membrane protease; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the peptidase M48B family. | 0.634 |
| prsW | rseP | BSU22940 | BSU16560 | Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...] | Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane. | 0.920 |
| prsW | rsiW | BSU22940 | BSU01740 | Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...] | anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...] | 0.993 |
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