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Molecular architecture and function of the Omp85 family of proteins
Author(s) -
Gentle Ian E.,
Burri Lena,
Lithgow Trevor
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04906.x
Subject(s) - bacterial outer membrane , periplasmic space , biology , outer membrane efflux proteins , protein family , microbiology and biotechnology , function (biology) , membrane protein , bcl 2 family , genetics , membrane , escherichia coli , gene , apoptosis , programmed cell death
Summary Omp85 is a protein found in Gram‐negative bacteria where it serves to integrate proteins into the bacterial outer membrane. Members of the Omp85 family of proteins are defined by the presence of two domains: an N‐terminal, periplasmic domain rich in POTRA repeats and a C‐terminal beta‐barrel domain embedded in the outer membrane. The widespread distribution of Omp85 family members together with their fundamental role in outer membrane assembly suggests the ancestral Omp85 arose early in the evolution of prokaryotic cells. Mitochondria, derived from an ancestral bacterial endosymbiont, also use a member of the Omp85 family to assemble proteins in their outer membranes. More distant relationships are seen between the Omp85 family and both the core proteins in two‐partner secretion systems and the Toc75 family of protein translocases found in plastid outer envelopes. Aspects of the ancestry and molecular architecture of the Omp85 family of proteins is providing insight into the mechanism by which proteins might be integrated and assembled into bacterial outer membranes.