RRC ID 35473
Author Lütticke C, Hauske P, Lewandrowski U, Sickmann A, Kaiser M, Ehrmann M.
Title E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
Journal Mol Biosyst
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.
Volume 8(6)
Pages 1775-82
Published 2012-6
DOI 10.1039/c2mb05506f
PMID 22491786
MeSH Cell Membrane / chemistry Cell Membrane / metabolism Cytoskeletal Proteins / chemistry Cytoskeletal Proteins / metabolism Dipeptides / chemistry Dipeptides / metabolism* Escherichia coli Proteins / chemistry Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism* Hydrolysis Metalloproteases / chemistry Metalloproteases / genetics Metalloproteases / metabolism*
IF 2.759
Times Cited 5
Prokaryotes E. coli NA