node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
htrA | nlpI | STM0209 | STM3281 | 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 [...] | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | 0.415 |
htrA | ompR | STM0209 | STM3502 | 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 [...] | Response regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity). | 0.554 |
htrA | pal | STM0209 | STM0749 | 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 [...] | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 0.625 |
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 [...] | 0.918 |
msbB | tolB | STM1889 | STM0748 | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. | 0.700 |
msbB | tolR | STM1889 | STM0746 | Myristoyl transferase in lipid A biosynthesis; Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)- lipid A. | Tol protein, role in outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. | 0.864 |
nlpI | htrA | STM3281 | STM0209 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (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 [...] | 0.415 |
nlpI | pal | STM3281 | STM0749 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 0.428 |
nlpI | rseA | STM3281 | STM2639 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (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 [...] | 0.705 |
nlpI | tolR | STM3281 | STM0746 | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | Tol protein, role in outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. | 0.774 |
ompR | htrA | STM3502 | STM0209 | Response regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (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 [...] | 0.554 |
ompR | rseA | STM3502 | STM2639 | Response regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (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 [...] | 0.659 |
pal | htrA | STM0749 | STM0209 | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | 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 [...] | 0.625 |
pal | nlpI | STM0749 | STM3281 | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | 0.428 |
pal | tolB | STM0749 | STM0748 | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. | 0.999 |
pal | tolQ | STM0749 | STM0745 | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Tol protein, membrane-spanning inner membrane protein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. | 0.992 |
pal | tolR | STM0749 | STM0746 | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Tol protein, role in outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. | 0.992 |
pal | vacJ | STM0749 | STM2392 | Tol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Similar to E. coli lipoprotein precursor (AAC75406.1); Blastp hit to AAC75406.1 (251 aa), 94% identity in aa 1 - 251. | 0.508 |
rseA | htrA | STM2639 | STM0209 | 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 [...] | 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 [...] | 0.918 |
rseA | nlpI | STM2639 | STM3281 | 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 [...] | Lipoprotein, cell division; May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity). | 0.705 |