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Information on EC 3.4.21.B50 - DegQ peptidase
for references in articles please use BRENDA:EC3.4.21.B50
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B50 DegQ peptidase
The enzyme appears in viruses and cellular organisms
Synonyms
deg2 protease, more
top
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
B3234
-
-
-
-
DegQ
HhoA peptidase
-
-
-
-
S01.274
-
-
-
-
S01.482
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arc-st11 repressor + H2O
?
-
Substrates: cleavage sites: Val22-/-Arg23, Val25-/-Ala25 and Val41-/-Met42
Products: -
Products: -
?
casein + H2O
hydrolyzed casein
Substrates: endoprotease, active serine protease whose activity requires the integrity of the catalytic site and the PDZ domains
Products: -
Products: -
?
lambda-repressor variant 105 + H2O
?
-
Substrates: cleavage sites: Val36-/-Ala37, Val71-/-Ser72, Ile84-/-Tyr85, Val91-/-Ser92
Products: -
Products: -
?
DPMFKLV-4-methylcoumaryl-7-amide + H2O
?
Substrates: -
Products: -
Products: -
?
DPMFKLV-4-methylcoumaryl-7-amide + H2O
?
Substrates: -
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: DegQ controls the transition from flagellum formation to biofilm formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: degQ is required for plipastatin synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified DegQ protein stimulated phosphotransfer from phospho-DegS to DegU in vitro
Products: -
Products: -
?
additional information
?
-
-
Substrates: the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: model substrates are cleaved at discrete Val/Xaa or Ile/Xaa sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: wild type DegQ exhibits a much lower proteolytic activity, and thus higher chaperone-like activity, than DegP
Products: -
Products: -
?
additional information
?
-
-
Substrates: DegQ does not degrade native bovine serum albumin and reductively unfolded lysozyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: DegQ is not essential for serovar typhimurium pathogenesis but may play a small role during salmonella growth at systemic sites
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
E-cadherin + H2O
?
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: DegQ controls the transition from flagellum formation to biofilm formation
Products: -
Products: -
?
additional information
?
-
-
Substrates: degQ is required for plipastatin synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
Products: -
Products: -
?
additional information
?
-
-
Substrates: the genes degQ, pps, and lpa-8 are responsible for conversion of Bacillus subtilis 168 to plipastatin production
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: wild type DegQ exhibits a much lower proteolytic activity, and thus higher chaperone-like activity, than DegP
Products: -
Products: -
?
additional information
?
-
-
Substrates: DegQ is not essential for serovar typhimurium pathogenesis but may play a small role during salmonella growth at systemic sites
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
exhibits more than 70% of the maximum activity over the pH range of 5 to 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 55
exhibits more than 70% of the maximum activity over the temperature range of 40 to 55°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain T4, a pathogenic strain isolated from diseased fish
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides
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
-
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
-
the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides
-
malfunction
Bacillus subtilis NCD-2
-
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
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
-
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
-
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
Bacillus subtilis NCD-2
-
DegQ may be an important regulatorof fengycin production and biofilm formation in Bacillus subtilis NCD-2
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). B7UJW6_ECO27
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
455
1
47216
TrEMBL
-
Q5ZVV9_LEGPH
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
466
1
49612
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
600000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
additional information
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
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion technique. The best crystals are obtained when using 100 mM citrate (pH 5.5) and 17.5% polyethylene glycol 400 or 100 mM sodium acetate (pH 4.5), 50 mM CdCl2 and 28% polyethylene glycol 400 as reservoir solutions. Crystal structures of inactive 3-mers and active 12-mers of DegQ reveal molecular details of elements of a conserved allosteric activation cascade that defines distinct protease ON and OFF states
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
engineering of a xylose-inducible DegQ strain SQR9XYQ to improve the biocontrol activity. In this strain, the phosphorylation of DegU can be gradually activated by xylose, and biofilm formation, antibiotic expression, colonization activity, and biocontrol efficiency are improved compared with the wild-type strain
additional information
-
engineering of a xylose-inducible DegQ strain SQR9XYQ to improve the biocontrol activity. In this strain, the phosphorylation of DegU can be gradually activated by xylose, and biofilm formation, antibiotic expression, colonization activity, and biocontrol efficiency are improved compared with the wild-type strain
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
medicine
the purified recombinant DegQVh is a protective immunogen that could confer protection upon fish against infection by Vibrio harveyi. In order to improve the efficiency of DegQVh as a vaccine, a genetic construct in the form of the plasmid pAQ1 is built, in which the DNA encoding the processed DegQVh protein is fused with the DNA encoding the secretion region of AgaV, an extracellular beta-agarase. The Escherichia coli strain harboring pAQ1 can express and secrete the chimeric DegQVh protein into the culture supernatant. Vaccination of fish with viable Escherichia coli expressing chimeric degQVh significantly enhanced the survival of fish against Vibrio harveyi challenge, which is possibly due to the relatively prolonged exposure of the immune system to the recombinant antigen produced constitutively
agriculture
-
engineering of a xylose-inducible DegQ strain SQR9XYQ to improve the biocontrol activity. In this strain, the phosphorylation of DegU can be gradually activated by xylose, and biofilm formation, antibiotic expression, colonization activity, and biocontrol efficiency are improved compared with the wild-type strain
agriculture
-
engineering of a xylose-inducible DegQ strain SQR9XYQ to improve the biocontrol activity. In this strain, the phosphorylation of DegU can be gradually activated by xylose, and biofilm formation, antibiotic expression, colonization activity, and biocontrol efficiency are improved compared with the wild-type strain
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Escherichia coli O127:H6 (B7UJW6), Escherichia coli O127:H6 E2348/69 (B7UJW6), Proteus mirabilis (B4EXL6), 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
Xu, Z.; Xie, J.; Zhang, H.; Wang, D.; Shen, Q.; Zhang, R.
Enhanced control of plant wilt disease by a xylose-inducible degq gene engineered into Bacillus velezensis strain SQR9XYQ
Phytopathology
109
36-43
2019
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens SQR9
brenda
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