E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds

Lütticke, Christiane, Hauske, Patrick, Lewandrowski, Urs, Sickmann, Albert, Kaiser, Markus and Ehrmann, Michael ORCID: https://orcid.org/0000-0002-1927-260X 2012. E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds. Molecular BioSystems 8 (6) , pp. 1775-1782. 10.1039/c2mb05506f

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Abstract

YggG is a conserved lipoprotein localized to the outer membrane of Gram negative bacteria. Even though the expressed open reading frame has been identified previously, the Escherichia coli protein remained uncharacterized. We report that YggG of E. coli is a metalloprotease that cleaves its targets preferentially between Phe–Phe residues. Since the yggG promoter is upregulated when bacteria are subjected to media of low osmolarity, YggG was named LoiP (low osmolarity induced protease). LoiP has an intramolecular disulfide (S–S) bond that is formed even in the absence of the periplasmic oxido-reductase DsbA and proper membrane localization of LoiP can depend on another putative metalloprotease, YfgC.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > QH Natural history
Publisher:	Royal Society of Chemistry
ISSN:	1742-206X
Last Modified:	25 Oct 2022 09:02
URI:	https://orca.cardiff.ac.uk/id/eprint/56924

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