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Escherichia coli signal peptide peptidase a is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the s49 protease family
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Crystal structure of a bacterial signal peptide peptidase
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The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP
Janine Heinrich et al.
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Characterization of the sequence specificity determinants required for processing and control of sex pheromone by the intramembrane protease Eep and the plasmid-encoded protein PrgY
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Structure of a site-2 protease family intramembrane metalloprotease
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A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase
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RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
Y Akiyama et al.
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Fine-tuning of the Escherichia coli σE envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA
IL Grigorova et al.
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The Bacillus subtilisσW anti-sigma factor RsiW is degraded by intramembrane proteolysis through YluC
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YaeL proteolysis of RseA is controlled by the PDZ domain of YaeL and a Gln-rich region of RseA
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OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
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Biochemical characterization of a mutationallv altered protein translocase: Proton motive force stimulation of the initiation phase of translocation
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YaeL (EcfE) activates the σE pathway of stress response through a site-2 cleavage of anti-σE, RseA
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DegS and YaeL participate sequentially in the cleavage of RseA to activate the σE-dependent extracytoplasmic stress response
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ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
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