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Arc-st11 repressor + H2O
?
-
cleavage sites: Val22-/-Arg23, Val25-/-Ala25 and Val41-/-Met42
-
-
?
casein + H2O
hydrolyzed casein
endoprotease, active serine protease whose activity requires the integrity of the catalytic site and the PDZ domains
-
-
?
DPMFKLV-4-methylcoumaryl-7-amide + H2O
?
lambda-repressor variant 105 + H2O
?
-
cleavage sites: Val36-/-Ala37, Val71-/-Ser72, Ile84-/-Tyr85, Val91-/-Ser92
-
-
?
OmpA protein + H2O
?
-
-
-
-
?
unfolded bovine serum albumin + H2O
?
-
-
-
-
?
additional information
?
-
beta-casein + H2O
?
the enzyme is able to specifically degrade beta-casein but not alpha-casein
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
DPMFKLV-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
DPMFKLV-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
E-cadherin + H2O
?
-
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
additional information
?
-
the enzyme shows chaperone-like activity, its presence reduces the aggregation of the DTT-denatured lysozyme
-
-
?
additional information
?
-
-
DegQ is responsible for differences in expression of the bacillomycin D operon (bmy) in Bacillus subtilis MO1099 and Bacillus amyloliquefaciens FZB42. Transcription of degQ in FZB42 is driven by the stronger sigmaA promoter version, whereas Bacillus subtilis MO1099, a derivative of the strain 168, carries the defective degQ promoter version
-
-
?
additional information
?
-
-
DegQ is responsible for differences in expression of the bacillomycin D operon (bmy) in Bacillus subtilis MO1099 and Bacillus amyloliquefaciens FZB42. Transcription of degQ in FZB42 is driven by the stronger sigmaA promoter version, whereas Bacillus subtilis MO1099, a derivative of the strain 168, carries the defective degQ promoter version
-
-
?
additional information
?
-
-
DegQ controls the transition from flagellum formation to biofilm formation
-
-
?
additional information
?
-
-
degQ is required for plipastatin synthesis
-
-
?
additional information
?
-
-
the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
-
-
?
additional information
?
-
-
purified DegQ protein stimulated phosphotransfer from phospho-DegS to DegU in vitro
-
-
?
additional information
?
-
-
the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
-
-
?
additional information
?
-
-
DegQ may degrade transiently denatured proteins, unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and/or newly secreted proteins prior to folding and disulfide bond formation
-
-
?
additional information
?
-
-
model substrates are cleaved at discrete Val/Xaa or Ile/Xaa sites
-
-
?
additional information
?
-
-
wild type DegQ exhibits a much lower proteolytic activity, and thus higher chaperone-like activity, than DegP
-
-
?
additional information
?
-
-
DegQ does not degrade native bovine serum albumin and reductively unfolded lysozyme
-
-
?
additional information
?
-
-
DegQ is not essential for serovar typhimurium pathogenesis but may play a small role during salmonella growth at systemic sites
-
-
?
additional information
?
-
recombinant DegQVh can not degrade bovine serum albumin and collagen. The purified recombinant DegQVh is a protective immunogen that could confer protection upon fish against infection by Vibrio harveyi
-
-
?
additional information
?
-
-
recombinant DegQVh can not degrade bovine serum albumin and collagen. The purified recombinant DegQVh is a protective immunogen that could confer protection upon fish against infection by Vibrio harveyi
-
-
?
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beta-casein + H2O
?
-
-
-
-
?
OmpA protein + H2O
?
-
-
-
-
?
additional information
?
-
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
E-cadherin + H2O
?
infection of epithelial cells results in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin in the supernatants of infected cells. E-cadherin cleavage is an important step in bacterial pathogenesis
-
-
?
additional information
?
-
-
DegQ is responsible for differences in expression of the bacillomycin D operon (bmy) in Bacillus subtilis MO1099 and Bacillus amyloliquefaciens FZB42. Transcription of degQ in FZB42 is driven by the stronger sigmaA promoter version, whereas Bacillus subtilis MO1099, a derivative of the strain 168, carries the defective degQ promoter version
-
-
?
additional information
?
-
-
DegQ is responsible for differences in expression of the bacillomycin D operon (bmy) in Bacillus subtilis MO1099 and Bacillus amyloliquefaciens FZB42. Transcription of degQ in FZB42 is driven by the stronger sigmaA promoter version, whereas Bacillus subtilis MO1099, a derivative of the strain 168, carries the defective degQ promoter version
-
-
?
additional information
?
-
-
DegQ controls the transition from flagellum formation to biofilm formation
-
-
?
additional information
?
-
-
degQ is required for plipastatin synthesis
-
-
?
additional information
?
-
-
the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
-
-
?
additional information
?
-
-
the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
-
-
?
additional information
?
-
-
DegQ may degrade transiently denatured proteins, unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and/or newly secreted proteins prior to folding and disulfide bond formation
-
-
?
additional information
?
-
-
wild type DegQ exhibits a much lower proteolytic activity, and thus higher chaperone-like activity, than DegP
-
-
?
additional information
?
-
-
DegQ is not essential for serovar typhimurium pathogenesis but may play a small role during salmonella growth at systemic sites
-
-
?
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additional information
The Deg2 protease domain consists of a catalytic triad comprising His159, Asp190, and Ser268. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state
malfunction
-
the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides
malfunction
-
compared with the wild-type strain NCD-2, the degQ-null mutant has decreased extracellular protease and cellulase activities as well as antifungal ability against the growth of Babillus cinerea in vitro. The lipopeptides from the degQ-null mutant also have significantly decreased antifungal activity against Botrytis cinerea in vitro and in vivo. degQ-null mutant have a flatter colony phenotype and significantly decreased biofilm formation ability relative to the wild-type strain. The degQ-null mutant shows decreased fengycin production
malfunction
-
in domesticated Bacillus subtilis a promoter mutation decreases the rate of degQ transcription. The resulting low level of DegQ decreases DegU phosphorylation, relieving repression at the srfA promoter. As a result more ComS is synthesized and the degradation of ComK by MecA/ClpCP is decreased
malfunction
-
the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides
-
malfunction
-
compared with the wild-type strain NCD-2, the degQ-null mutant has decreased extracellular protease and cellulase activities as well as antifungal ability against the growth of Babillus cinerea in vitro. The lipopeptides from the degQ-null mutant also have significantly decreased antifungal activity against Botrytis cinerea in vitro and in vivo. degQ-null mutant have a flatter colony phenotype and significantly decreased biofilm formation ability relative to the wild-type strain. The degQ-null mutant shows decreased fengycin production
-
physiological function
-
DegQ does not act as a functional homolog of DegP and plays no role in outer membrane protein biogenesis in Neisseria meningitides
physiological function
the enzyme's proteolytic activity in the chloroplast stroma is required to maintain the efficiency of photosynthetic machinery during stress, the enzyme exhibits dual protease-chaperone activities
physiological function
-
DegQ may be an important regulatorof fengycin production and biofilm formation in Bacillus subtilis NCD-2
physiological function
E-cadherin cleavage is an important step in bacterial pathogenesis
physiological function
E-cadherin cleavage is an important step in bacterial pathogenesis
physiological function
-
the regulation of the K-state in undomesticated strains of Bacillus subtilis requires the proper ratio of phosphorylated undunphosphorylated DegU, in accordance with the view that this protein acts as a rheostat for development
physiological function
-
E-cadherin cleavage is an important step in bacterial pathogenesis
-
physiological function
-
DegQ does not act as a functional homolog of DegP and plays no role in outer membrane protein biogenesis in Neisseria meningitides
-
physiological function
-
E-cadherin cleavage is an important step in bacterial pathogenesis
-
physiological function
-
DegQ may be an important regulatorof fengycin production and biofilm formation in Bacillus subtilis NCD-2
-
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hexamer
-
6 * 50000, SDS-PAGE
hexamer or dodecamer
hexameric structure of mature enzyme, the Deg2 hexamer exists predominantly during substrate incubation in a resting state,the large oligomeric state is the active state, model of oligomeric state change, overview
trimer
-
substrate-free form
dodecamer
-
12 * 50000, SDS-PAGE
dodecamer
-
substrate-containing form, 12 * 50000, SDS-PAGE
dodecamer
-
12 * 48000-50000, dynamic light-scattering, DegQ assembles into large, cage-like dodecamers that form independently of unfolded substrate proteins. Dodecamer-formation is essential for the degradation of substrate proteins but not for the chaperone activity of DegQ
additional information
structure-function analysis of the dimerization interface between Deg2 trimers, overview. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state. Because loop JK lies outside the hexamer shell, it provides protection for the loop LA-PDZ2 interface from solvents and may play a role in changes in the oligomeric enzyme state
additional information
DegQLp forms predominantly trimers in the substrate-free state. In vitro, oligomerization is influenced by the pH of the protein solution and the presence of co-purified peptides binding to the PDZ1 and/or protease site. Misfolded proteins or peptides promote the assembly of protease active 12- or 24-mers the assembly of proteolytically active
additional information
-
DegQLp forms predominantly trimers in the substrate-free state. In vitro, oligomerization is influenced by the pH of the protein solution and the presence of co-purified peptides binding to the PDZ1 and/or protease site. Misfolded proteins or peptides promote the assembly of protease active 12- or 24-mers the assembly of proteolytically active
-
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Kolmar, H.; Waller, P.R.; Sauer, R.T.
The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation
J. Bacteriol.
178
5925-5929
1996
Escherichia coli
brenda
Tsuge, K.; Ano, T.; Hirai, M.; Nakamura, Y.; Shoda, M.
The genes degQ, pps, and lpa-8 (sfp) are responsible for conversion of Bacillus subtilis 168 to plipastatin production
Antimicrob. Agents Chemother.
43
2183-2192
1999
Bacillus subtilis, Bacillus subtilis 168
brenda
Koumoutsi, A.; Chen. X.H.
Vater, J.; Borriss, R.: DegU and YczE positively regulate the synthesis of bacillomycin D by Bacillus amyloliquefaciens strain FZB42
Appl. Environ. Microbiol.
73
6953-6964
2007
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens FZB42
brenda
Zhang W.W.
Sun, K.; Cheng, S.; Sun, L.: Characterization of DegQVh, a serine protease and a protective immunogen from a pathogenic Vibrio harveyi strain
Appl. Environ. Microbiol.
74
6254-6262
2008
Vibrio harveyi (B6CND6), Vibrio harveyi
brenda
Farn, J.; Roberts, M.
Effect of inactivation of the HtrA-like serine protease DegQ on the virulence of Salmonella enterica serovar Typhimurium in mice
Infect. Immun.
72
7357-7359
2004
Salmonella enterica
brenda
Yohannes, E.; Barnhart, D.M.; Slonczewski, J.L.
pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12
J. Bacteriol.
186
192-199
2004
Escherichia coli
brenda
Tsuge, K.; Matsui, K.; Itaya, M.
Production of the non-ribosomal peptide plipastatin in Bacillus subtilis regulated by three relevant gene blocks assembled in a single movable DNA segment
J. Biotechnol.
129
592-603
2007
Bacillus subtilis
brenda
Kobayashi, K.
Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis
Mol. Microbiol.
66
395-409
2007
Bacillus subtilis
brenda
Summerfield, T.C.; Eaton-Rye, J.J.; Sherman, L.A.
Global gene expression of a delta PsbO:delta PsbU mutant and a spontaneous revertant in the cyanobacterium Synechocystis sp. strain PCC 6803
Photosynth. Res.
94
265-274
2007
Synechocystis sp.
brenda
Volokhina, E.B.; Grijpstra, J.; Stork, M.; Schilders, I.; Tommassen, J.; Bos, M.P.
Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis
J. Bacteriol.
193
1612-1621
2011
Neisseria meningitidis, Neisseria meningitidis HB-1
brenda
Wrase, R.; Scott, H.; Hilgenfeld, R.; Hansen, G.
The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies
Proc. Natl. Acad. Sci. USA
108
10490-10495
2011
Legionella fallonii
brenda
Bai, X.C.; Pan, X.J.; Wang, X.J.; Ye, Y.Y.; Chang, L.F.; Leng, D.; Lei, J.; Sui, S.F.
Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins
Structure
19
1328-1337
2011
Escherichia coli
brenda
Sun, R.; Fan, H.; Gao, F.; Lin, Y.; Zhang, L.; Gong, W.; Liu, L.
Crystal structure of Arabidopsis Deg2 protein reveals an internal PDZ ligand locking the hexameric resting state
J. Biol. Chem.
287
37564-37569
2012
Arabidopsis thaliana (O92261)
brenda
Abfalter, C.; Schubert, M.; Gtz, C.; Schmidt, T.; Posselt, G.; Wessler, S.
HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogens
Cell Commun. Signal.
14
30
2016
Proteus mirabilis (B4EXL6), Escherichia coli O127:H6 (B7UJW6), Escherichia coli O127:H6 E2348/69 (B7UJW6), Proteus mirabilis HI4320 (B4EXL6)
brenda
Miras, M.; Dubnau, D.
A DegU-P and DegQ-dependent regulatory pathway for the K-state in Bacillus subtilis
Front. Microbiol.
7
1868
2016
Bacillus subtilis
brenda
Schubert, A.; Wrase, R.; Hilgenfeld, R.; Hansen, G.
Structures of DegQ from Legionella pneumophila define distinct on and off states
J. Mol. Biol.
427
2840-2851
2015
Legionella pneumophila subsp. pneumophila (Q5ZVV9), Legionella pneumophila subsp. pneumophila ATCC 33152 (Q5ZVV9)
brenda
Wang, P.; Guo, Q.; Ma, Y.; Li, S.; Lu, X.; Zhang, X.; Ma, P.
DegQ regulates the production of fengycins and biofilm formation of the biocontrol agent Bacillus subtilis NCD-2
Microbiol. Res.
178
42-50
2015
Bacillus subtilis, Bacillus subtilis NCD-2
brenda