| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| degQ | degS | STM3348 | STM3349 | Similar to E. coli serine endoprotease (AAC76266.1); Blastp hit to AAC76266.1 (455 aa), 89% identity in aa 1 - 455; Belongs to the peptidase S1C family. | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | 0.712 |
| degQ | rseA | STM3348 | STM2639 | Similar to E. coli serine endoprotease (AAC76266.1); Blastp hit to AAC76266.1 (455 aa), 89% identity in aa 1 - 455; Belongs to the peptidase S1C family. | Anti sigma E (sigma 24) factor, negative regulator; 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 cytop [...] | 0.855 |
| degQ | yaeL | STM3348 | STM0223 | Similar to E. coli serine endoprotease (AAC76266.1); Blastp hit to AAC76266.1 (455 aa), 89% identity in aa 1 - 455; Belongs to the peptidase S1C family. | Putative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. | 0.664 |
| degS | degQ | STM3349 | STM3348 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Similar to E. coli serine endoprotease (AAC76266.1); Blastp hit to AAC76266.1 (455 aa), 89% identity in aa 1 - 455; Belongs to the peptidase S1C family. | 0.712 |
| degS | rpoE | STM3349 | STM2640 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | 0.886 |
| degS | rseA | STM3349 | STM2639 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Anti sigma E (sigma 24) factor, negative regulator; 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 cytop [...] | 0.997 |
| degS | rseB | STM3349 | STM2638 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Anti sigma E (sigma 24) factor, negative regulator; Similar to E. coli regulates activity of sigma-E factor (AAC75624.1); Blastp hit to AAC75624.1 (318 aa), 89% identity in aa 1 - 318. | 0.920 |
| degS | rseC | STM3349 | STM2637 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Similar to E. coli sigma-E factor, negative regulatory protein (AAC75623.1); Blastp hit to AAC75623.1 (159 aa), 81% identity in aa 1 - 159. | 0.746 |
| degS | yaeL | STM3349 | STM0223 | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | Putative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. | 0.977 |
| htrA | rpoE | STM0209 | STM2640 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | 0.888 |
| htrA | rseA | STM0209 | STM2639 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Anti sigma E (sigma 24) factor, negative regulator; 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 cytop [...] | 0.967 |
| htrA | rseB | STM0209 | STM2638 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Anti sigma E (sigma 24) factor, negative regulator; Similar to E. coli regulates activity of sigma-E factor (AAC75624.1); Blastp hit to AAC75624.1 (318 aa), 89% identity in aa 1 - 318. | 0.673 |
| htrA | rseC | STM0209 | STM2637 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Similar to E. coli sigma-E factor, negative regulatory protein (AAC75623.1); Blastp hit to AAC75623.1 (159 aa), 81% identity in aa 1 - 159. | 0.418 |
| htrA | yaeL | STM0209 | STM0223 | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | Putative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. | 0.840 |
| rpoE | degS | STM2640 | STM3349 | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | Periplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. | 0.886 |
| rpoE | htrA | STM2640 | STM0209 | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | Periplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] | 0.888 |
| rpoE | rseA | STM2640 | STM2639 | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | Anti sigma E (sigma 24) factor, negative regulator; 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 cytop [...] | 0.999 |
| rpoE | rseB | STM2640 | STM2638 | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | Anti sigma E (sigma 24) factor, negative regulator; Similar to E. coli regulates activity of sigma-E factor (AAC75624.1); Blastp hit to AAC75624.1 (318 aa), 89% identity in aa 1 - 318. | 0.994 |
| rpoE | rseC | STM2640 | STM2637 | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | Similar to E. coli sigma-E factor, negative regulatory protein (AAC75623.1); Blastp hit to AAC75623.1 (159 aa), 81% identity in aa 1 - 159. | 0.959 |
| rpoE | yaeL | STM2640 | STM0223 | Sigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). | Putative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. | 0.773 |
