| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| nprB | yitM | BSU11100 | BSU11040 | Extracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.658 |
| nprB | yitO | BSU11100 | BSU11055 | Extracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. | Putative integral inner membrane protein with HTTM domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.670 |
| nprB | yitP | BSU11100 | BSU11070 | Extracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 6289325. | 0.625 |
| nprB | yitQ | BSU11100 | BSU11080 | Extracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.755 |
| nprB | yitR | BSU11100 | BSU11090 | Extracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.830 |
| nprB | yizB | BSU11100 | BSU11079 | Extracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. | Putative DNA/RNA binding protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. | 0.706 |
| sdpA | sdpB | BSU33750 | BSU33760 | Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Exporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | 0.998 |
| sdpA | sdpI | BSU33750 | BSU33780 | Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | 0.426 |
| sdpA | yitM | BSU33750 | BSU11040 | Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.512 |
| sdpA | yitO | BSU33750 | BSU11055 | Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Putative integral inner membrane protein with HTTM domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.847 |
| sdpB | sdpA | BSU33760 | BSU33750 | Exporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | 0.998 |
| sdpB | sdpI | BSU33760 | BSU33780 | Exporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | 0.490 |
| sdpB | yitM | BSU33760 | BSU11040 | Exporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.588 |
| sdpB | yitP | BSU33760 | BSU11070 | Exporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 6289325. | 0.776 |
| sdpI | sdpA | BSU33780 | BSU33750 | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | 0.426 |
| sdpI | sdpB | BSU33780 | BSU33760 | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | Exporter of killing factor SpbC; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation. | 0.490 |
| sdpI | sdpR | BSU33780 | BSU33790 | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | Transcriptional regulator (ArsR family); Represses the transcription of the sdpIR operon and of several other operons that probably contribute to delaying commitment to sporulation. | 0.999 |
| sdpI | yitM | BSU33780 | BSU11040 | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.496 |
| sdpI | yitQ | BSU33780 | BSU11080 | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.487 |
| sdpI | yitR | BSU33780 | BSU11090 | Integral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. | Hypothetical protein; Evidence 5: No homology to any previously reported sequences. | 0.605 |