| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| comC | dprA | BSU28070 | BSU16110 | Membrane protease and transmethylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue; Belongs to the peptidase A24 family. | DNA processing Smf single strand binding protein; Protein that helps load RecA onto ssDNA during transformation. Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA. Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments. RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. | 0.967 |
| comC | maf | BSU28070 | BSU28050 | Membrane protease and transmethylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue; Belongs to the peptidase A24 family. | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.749 |
| comC | radC | BSU28070 | BSU28040 | Membrane protease and transmethylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue; Belongs to the peptidase A24 family. | Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.737 |
| dprA | comC | BSU16110 | BSU28070 | DNA processing Smf single strand binding protein; Protein that helps load RecA onto ssDNA during transformation. Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA. Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments. RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. | Membrane protease and transmethylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue; Belongs to the peptidase A24 family. | 0.967 |
| dprA | radA | BSU16110 | BSU00870 | DNA processing Smf single strand binding protein; Protein that helps load RecA onto ssDNA during transformation. Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA. Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments. RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. | DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. | 0.690 |
| dprA | radC | BSU16110 | BSU28040 | DNA processing Smf single strand binding protein; Protein that helps load RecA onto ssDNA during transformation. Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA. Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments. RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. | Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.764 |
| maf | comC | BSU28050 | BSU28070 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Membrane protease and transmethylase; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue; Belongs to the peptidase A24 family. | 0.749 |
| maf | minC | BSU28050 | BSU28000 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | 0.819 |
| maf | minD | BSU28050 | BSU27990 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | ATPase activator of MinC; ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity); Belongs to the ParA family. MinD subfamily. | 0.638 |
| maf | mreB | BSU28050 | BSU28030 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Cell-shape determining protein; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization. The [...] | 0.910 |
| maf | mreC | BSU28050 | BSU28020 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Cell-shape determining protein; Involved in formation and maintenance of cell shape. Required for the formation of proper helical filaments of MreB and for cell wall synthesis in the cylindrical part of the cell leading to cell elongation; Belongs to the MreC family. | 0.922 |
| maf | mreD | BSU28050 | BSU28010 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Cell-shape determining protein; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (By similarity). | 0.864 |
| maf | radC | BSU28050 | BSU28040 | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.995 |
| minC | maf | BSU28000 | BSU28050 | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.819 |
| minC | minD | BSU28000 | BSU27990 | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | ATPase activator of MinC; ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity); Belongs to the ParA family. MinD subfamily. | 0.999 |
| minC | mreB | BSU28000 | BSU28030 | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | Cell-shape determining protein; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization. The [...] | 0.988 |
| minC | mreC | BSU28000 | BSU28020 | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | Cell-shape determining protein; Involved in formation and maintenance of cell shape. Required for the formation of proper helical filaments of MreB and for cell wall synthesis in the cylindrical part of the cell leading to cell elongation; Belongs to the MreC family. | 0.994 |
| minC | mreD | BSU28000 | BSU28010 | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | Cell-shape determining protein; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (By similarity). | 0.996 |
| minC | radC | BSU28000 | BSU28040 | Cell-division regulator (septum placement); Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells. | Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.847 |
| minD | maf | BSU27990 | BSU28050 | ATPase activator of MinC; ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity); Belongs to the ParA family. MinD subfamily. | Septum formation DNA-binding protein; Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo- UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | 0.638 |