| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| acuC | dnaK | BSU29710 | BSU25470 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.767 |
| acuC | htpG | BSU29710 | BSU39820 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.847 |
| acuC | ndk | BSU29710 | BSU22730 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.776 |
| acuC | pksJ | BSU29710 | BSU17180 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.728 |
| acuC | ppiB | BSU29710 | BSU23360 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Peptidyl-prolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.827 |
| acuC | yvyF | BSU29710 | BSU35440 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Putative regulator of flagella formation; May be involved in the assembly, structure, or function of the flagellum. May polymerize to form a filamentous structure that is part of the flagellum. | 0.904 |
| dapB | ppiB | BSU22490 | BSU23360 | (4S)-4-hydroxy-2,3,4, 5-tetrahydro-(2S)-dipicolinic acid (HTPA) dehydratase reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. | Peptidyl-prolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.936 |
| dnaK | acuC | BSU25470 | BSU29710 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | 0.767 |
| dnaK | fusA | BSU25470 | BSU01120 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). | 0.968 |
| dnaK | groES | BSU25470 | BSU06020 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.999 |
| dnaK | htpG | BSU25470 | BSU39820 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.999 |
| dnaK | ndk | BSU25470 | BSU22730 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.702 |
| dnaK | pksJ | BSU25470 | BSU17180 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.849 |
| dnaK | pksN | BSU25470 | BSU17210 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. | 0.769 |
| dnaK | ppiB | BSU25470 | BSU23360 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Peptidyl-prolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.912 |
| dnaK | yvyF | BSU25470 | BSU35440 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Putative regulator of flagella formation; May be involved in the assembly, structure, or function of the flagellum. May polymerize to form a filamentous structure that is part of the flagellum. | 0.427 |
| fusA | dnaK | BSU01120 | BSU25470 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.968 |
| fusA | groES | BSU01120 | BSU06020 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.406 |
| fusA | htpG | BSU01120 | BSU39820 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.439 |
| fusA | ndk | BSU01120 | BSU22730 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). | Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. | 0.619 |