EC Number |
General Information |
Reference |
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3.4.21.B50 | 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 |
-, 754649 |
3.4.21.B50 | 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 |
753678 |
3.4.21.B50 | malfunction |
the absence of DegQ does not affect outer membrane protein biogenesis in Neisseria meningitides |
-, 717730 |
3.4.21.B50 | more |
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 |
732074 |
3.4.21.B50 | physiological function |
DegQ does not act as a functional homolog of DegP and plays no role in outer membrane protein biogenesis in Neisseria meningitides |
-, 717730 |
3.4.21.B50 | physiological function |
DegQ may be an important regulatorof fengycin production and biofilm formation in Bacillus subtilis NCD-2 |
-, 754649 |
3.4.21.B50 | physiological function |
E-cadherin cleavage is an important step in bacterial pathogenesis |
-, 753173 |
3.4.21.B50 | 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 |
732074 |
3.4.21.B50 | 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 |
753678 |