3.4.21.B50: DegQ peptidase
This is an abbreviated version!
For detailed information about DegQ peptidase, go to the full flat file.
Reaction
Synonyms
B3234, DEG2, Deg2 protease, DegQ, DegQVh, HhoA peptidase, S01.274, S01.482
ECTree
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General Information
General Information on EC 3.4.21.B50 - DegQ peptidase
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malfunction
physiological function
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
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the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides
malfunction
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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
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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
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the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides
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malfunction
Bacillus subtilis NCD-2
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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
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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
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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
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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
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E-cadherin cleavage is an important step in bacterial pathogenesis
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physiological function
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DegQ does not act as a functional homolog of DegP and plays no role in outer membrane protein biogenesis in Neisseria meningitides
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physiological function
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E-cadherin cleavage is an important step in bacterial pathogenesis
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physiological function
Bacillus subtilis NCD-2
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DegQ may be an important regulatorof fengycin production and biofilm formation in Bacillus subtilis NCD-2
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