degS

Signal transduction histidine-protein kinase/phosphatase DegS

386 amino acids

Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Acts as both a protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to DegU, and a protein phosphatase that dephosphorylates phospho-DegU (By similarity).

44.837 kDa

MPFKGLVVQVADPQTLDKIIDKTLDTVGKSREQIFEISEQSRNEYVSLEQELQEVRMKVAEIIDQSDRAEVHARFARNRLAEVSKQFHRYSNEEIRKVYEQANELQVKLALLQQEEQQLRDRRDAIERRLLNLKDTIERAEELVGQMTVVYNFLTGDLRQVGEALEDAREKQAFGLQIIQAQEEERRKLSREIHDGPAQMMANVLLRSELVERIYHDKGIDEALKEIRDLRKMVKSSLAEVRRIIYDLRRMALDDLGLIPTLKKYVKTFEEHTGIFVDFKHIGKGERFPEHVEIALFRLVQEALQNTRKHAKASHVHVKIEEQKTKFTVVIKDNGKGFDQTEKKEGSFGLVGMKERVNMLKGQLVIRTKPNDGTTIIISIPITTEE

degS

Signal transduction histidine-protein kinase/phosphatase DegS

385 amino acids

Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Involved in the control of expression of different cellular functions, including production of degradative enzymes such as the neutral and alkaline proteases, flagellum formation and biofilm formation. Acts as both a protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to DegU, and a protein phosphatase that dephosphorylates phospho-DegU.

44.958 kDa

MNKTKMDSKVLDSILMKMLKTVDGSKDEVFQIGEQSRQQYEQLVEELKQIKQQVYEVIELGDKLEVQTRHARNRLSEVSRNFHRFSEEEIRNAYEKAHKLQVELTMIQQREKQLRERRDDLERRLLGLQEIIERSESLVSQITVVLNYLNQDLREVGLLLADAQAKQDFGLRIIEAQEEERKRVSREIHDGPAQMLANVMMRSELIERIFRDRGAEDGFQEIKNLRQNVRNALYEVRRIIYDLRPMALDDLGLIPTLRKYLYTTEEYNGKVKIHFQCIGETEDQRLAPQFEVALFRLAQEAVSNALKHSESEEITVKVEITKDFVILMIKDNGKGFDLKEAKEKKNKSFGLLGMKERVDLLEGTMTIDSKIGLGTFIMIKVPLSL

degS

Serine endoprotease DegS

356 amino acids

A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and heat shock-induced degradation of RseA but not for acid stress response in this strain.

Belongs to the peptidase S1C family.

37.795 kDa

MFVKLLRSVAIGLIVGAILLAVMPSLRKINPIAVPQFDSTDETPASYNFAVRRAAPAVVNVYNRSMNSTAHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINTKRTPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGLGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQQGSGMDPIQGIVVNEVTPNGPAALAGIQVNDLIISVNNKPAVSALETMDQVAEIRPGSVIPVVVMRDDKQLTFQVTVQEYPASN

degS

Serine endoprotease DegS

355 amino acids

A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA (By similarity).

Belongs to the peptidase S1C family.

37.581 kDa

MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN

degS

Serine endoprotease DegS

355 amino acids

A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA.

Belongs to the peptidase S1C family.

37.581 kDa

MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN

degS

Serine endoprotease DegS

340 amino acids

A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA (By similarity).

Belongs to the peptidase S1C family.

36.039 kDa

MLKKLFHSALWGLAAAGVILFAVPRLNNSNIFTSDDIISFKNAVRIASPAVVNVYNRSFSSASINDNDQLQVNNLGSGVIMSKDGYILTNKHLIQNADQIVVALQNGNIFEASLVGSDDLTDLAVLKIRADNLSTIPQNSARQAHVGDVVLAIGNPYNLGQSVSQGIISAIGRNAVGDSVGRQNFIQTDASINRGNSGGALINSAGELVGISTLSIGKTANEIAEGLNFAIPIDIANDVLRKIMRDGRVIRGYFGVQSDISSSSEEGIVITDVSPNSPAAKSGIQVGDVILKLNNQEGISAREMMQIIANTKPNSKVLVTILRLGKILQIPVVIEEFPVN