| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| dedD | dsbB | CH53_408 | CH53_3834 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | 0.706 |
| dedD | lptC | CH53_408 | CH53_2248 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | LPS export ABC transporter periplasmic protein LptC; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | 0.745 |
| dedD | mclA | CH53_408 | CH53_686 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | Hypothetical protein; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). 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, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrad [...] | 0.705 |
| dedD | metJ | CH53_408 | CH53_1906 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | Met Apo-repressor, MetJ family protein; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. | 0.611 |
| dedD | mutH | CH53_408 | CH53_2683 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | DNA mismatch repair endonuclease MutH; Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair. Belongs to the MutH family. | 0.726 |
| dedD | proQ | CH53_408 | CH53_4276 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | proP effector; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. Belongs to the ProQ family. | 0.746 |
| dedD | rraB | CH53_408 | CH53_1241 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | Regulator of ribonuclease activity B; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | 0.692 |
| dedD | slyX | CH53_408 | CH53_1501 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | slyX family protein; Belongs to the SlyX family. | 0.687 |
| dedD | syd | CH53_408 | CH53_2712 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | Protein syd; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family. | 0.747 |
| dedD | yciS | CH53_408 | CH53_3914 | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | Inner membrane protein yciS; Involved in the assembly of lipopolysaccharide (LPS). Belongs to the LapA family. | 0.673 |
| dsbB | dedD | CH53_3834 | CH53_408 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Sporulation related domain protein; Non-essential cell division protein that could be required for efficient cell constriction. | 0.706 |
| dsbB | lptC | CH53_3834 | CH53_2248 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | LPS export ABC transporter periplasmic protein LptC; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. | 0.763 |
| dsbB | mclA | CH53_3834 | CH53_686 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Hypothetical protein; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). 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, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrad [...] | 0.547 |
| dsbB | metJ | CH53_3834 | CH53_1906 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Met Apo-repressor, MetJ family protein; This regulatory protein, when combined with SAM (S- adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis; Belongs to the MetJ family. | 0.701 |
| dsbB | mutH | CH53_3834 | CH53_2683 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | DNA mismatch repair endonuclease MutH; Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair. Belongs to the MutH family. | 0.556 |
| dsbB | proQ | CH53_3834 | CH53_4276 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | proP effector; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. Belongs to the ProQ family. | 0.723 |
| dsbB | rraB | CH53_3834 | CH53_1241 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Regulator of ribonuclease activity B; Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. | 0.716 |
| dsbB | slyX | CH53_3834 | CH53_1501 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | slyX family protein; Belongs to the SlyX family. | 0.779 |
| dsbB | syd | CH53_3834 | CH53_2712 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Protein syd; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. Belongs to the Syd family. | 0.648 |
| dsbB | yciS | CH53_3834 | CH53_3914 | Disulfide bond formation DsbB family protein; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. | Inner membrane protein yciS; Involved in the assembly of lipopolysaccharide (LPS). Belongs to the LapA family. | 0.624 |