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• W1976965384 abstract "Members of the type V secretion family are among the most prevalent secreted proteins in Gram-negative bacteria. A subset of this family, including Pet, the prototypical member of the Enterobacteriaceae serine proteases, possess unusual signal peptides which can be divided into five regions termed N1 (charged), H1 (hydrophobic), N2, H2 and C (cleavage site) domains. The N1 and H1 regions, which the authors have named the extended signal peptide region (ESPR), demonstrate remarkable conservation. In contrast, the N2, H2 and C regions show significant variability, and are reminiscent of typical Sec-dependent signal sequences. Despite several investigations, the function of the ESPR remains obscure. Here, it is shown that proteins possessing the ESPR are translocated in a posttranslational fashion. The presence of the ESPR severely impairs inner membrane translocation. Mutational analysis suggests that the ESPR delays inner membrane translocation by adopting a particular conformation, or by interacting with a cytoplasmic or inner membrane co-factor, prior to inner membrane translocation." @default.
• W1976965384 created "2016-06-24" @default.
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• W1976965384 date "2007-01-01" @default.
• W1976965384 modified "2023-09-25" @default.
• W1976965384 title "A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism" @default.
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• W1976965384 doi "https://doi.org/10.1099/mic.0.29091-0" @default.
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