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The OmpA-like transmembrane domain Family [Function: Structural] Seed alignment | Full alignment | Pfam page | Pfam Wiki page | TC-DB page

This family includes homologs of the well characterized OmpA protein of Escherichia coli. Members of this family (similar to members of the OprF family) show a modular architecture which is composed of two distinctstructural domains: an N-terminal ß-barrel domain formed by 8 ß strands with short turns at the periplasmic ends and long flexible loops at the external ends that anchors the protein to the outer membrane; and a C-terminal domain that protrudes into the periplasmic space interacting with peptidoglycans. The C-terminal domain (named OmpA-like domain), is also found in a number of outer membrane lipoproteins, therefore it is not characteristic of ß-barrels. OmpA is largely expressed in the outer membrane of Escherichia coli and is required for bacterial conjugation and for maintenance of outer membrane stability. OmpA of E. coli K1 is a potential vaccine candidate because of its predominant contribution to bacterial pathogenesis and sub-cellular localization.There is also evidence that OmpA exhibits a small channel activity. There is a distant homology to Neisserial opacity (Opa) adhesins and members of the Ail/Lom/OmpX family but the barrels, though they possess the same number of strands (8), show different characteristics (shear numbers, inclination with respect to the membrane). A molecular-dynamics simulations of the full-length model of the OmpA dimer proposed by Robinson and co-workers revealed a large dimerization interface within the membrane environment, ensuring that the dimer is stable over the course of the simulations. The linker is flexible, expanding and contracting to pull the globular C-terminal domain up toward the membrane or push it down toward the periplasm, suggesting a possible mechanism for providing mechanical stability to the cell.

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Literature references

Microevolution in the major outer membrane protein OmpA of Acinetobacter baumannii
Microb Genom. 2020 Jun;6(6):e000381. doi: 10.1099/mgen.0.000381. Epub 2020 Jun 4.
PMID: 32496178

Magnetite-OmpA Nanobioconjugates as Cell-Penetrating Vehicles with Endosomal Escape Abilities
ACS Biomater Sci Eng. 2020 Jan 13;6(1):415-424. doi: 10.1021/acsbiomaterials.9b01214. Epub 2019 Dec 2.
PMID: 33463215

Folding of the ß-Barrel Membrane Protein OmpA into Nanodiscs
Biophys J. 2020 Jan 21;118(2):403-414. doi: 10.1016/j.bpj.2019.11.3381. Epub 2019 Nov 28.
PMID: 31843264

Outer Membrane Proteins OmpA, FhuA, OmpF, EstA, BtuB, and OmpX Have Unique Lipopolysaccharide Fingerprints
J Chem Theory Comput. 2019 Apr 9;15(4):2608-2619. doi: 10.1021/acs.jctc.8b01059. Epub 2019 Mar 21.
PMID: 30848905

Rational Design and Evaluation of an Artificial Escherichia coli K1 Protein Vaccine Candidate Based on the Structure of OmpA
Front Cell Infect Microbiol. 2018 May 23;8:172. doi: 10.3389/fcimb.2018.00172. eCollection 2018.
PMID: 29876324

The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition
J Biol Chem. 2018 Feb 23;293(8):2959-2973. doi: 10.1074/jbc.RA117.000349. Epub 2018 Jan 8.
PMID: 29311257

Insights into PG-binding, conformational change, and dimerization of the OmpA C-terminal domains from Salmonella enterica serovar Typhimurium and Borrelia burgdorferi
Protein Sci. 2017 Sep;26(9):1738-1748. doi: 10.1002/pro.3209. Epub 2017 Jun 19.
PMID: 28580643

Local and Global Dynamics in Klebsiella pneumoniae Outer Membrane Protein a in Lipid Bilayers Probed at Atomic Resolution
J Am Chem Soc. 2017 Feb 1;139(4):1590-1597. doi: 10.1021/jacs.6b11565. Epub 2017 Jan 20.
PMID: 28059506

Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane ß-Barrel OmpA
Biochemistry. 2017 Jan 10;56(1):47-60. doi: 10.1021/acs.biochem.6b00809. Epub 2016 Dec 21.
PMID: 28001375

Concatemers of Outer Membrane Protein A Take Detours in the Folding Landscape
Biochemistry. 2016 Dec 27;55(51):7123-7140. doi: 10.1021/acs.biochem.6b01153. Epub 2016 Dec 14.
PMID: 27973779

Full-Length OmpA: Structure, Function, and Membrane Interactions Predicted by Molecular Dynamics Simulations
Biophys J. 2016 Oct 18;111(8):1692-1702. doi: 10.1016/j.bpj.2016.09.009.
PMID: 27760356

Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association
PLoS One. 2015 Jul 21;10(7):e0132301. doi: 10.1371/journal.pone.0132301. eCollection 2015.
PMID: 26196893

The Borrelia afzelii outer membrane protein BAPKO_0422 binds human factor-H and is predicted to form a membrane-spanning ß-barrel
Biosci Rep. 2015 Jul 9;35(4):e00240. doi: 10.1042/BSR20150095.
PMID: 26181365

Detecting envelope stress by monitoring ß-barrel assembly
Cell. 2014 Dec 18;159(7):1652-64. doi: 10.1016/j.cell.2014.11.045.
PMID: 25525882

Recombinant outer membrane protein A fragments protect against Escherichia coli meningitis
J Microbiol Immunol Infect. 2016 Jun;49(3):329-34. doi: 10.1016/j.jmii.2014.07.012. Epub 2014 Oct 8.
PMID: 25305709

Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications
J Mol Biol. 2009 Jan 9;385(1):117-30. doi: 10.1016/j.jmb.2008.10.021. Epub 2008 Oct 15.
PMID: 18952100

A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance
Biochemistry. 2007 Feb 6;46(5):1128-40. doi: 10.1021/bi061265e.
PMID: 17260943

Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A
J Am Chem Soc. 2006 May 31;128(21):6947-51. doi: 10.1021/ja0608343.
PMID: 16719475

Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
Mol Microbiol. 2004 Feb;51(4):1027-37. doi: 10.1111/j.1365-2958.2003.03903.x.
PMID: 14763978

OmpA membrane domain as a tight-binding anchor for lipid bilayers
Chembiochem. 2002 May 3;3(5):463-6. doi: 10.1002/1439-7633(20020503)3:5<463::AID-CBIC463>3.0.CO;2-P.
PMID: 12007182

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
Nat Struct Biol. 2001 Apr;8(4):334-8. doi: 10.1038/86214.
PMID: 11276254

High-resolution structure of the OmpA membrane domain
J Mol Biol. 2000 Apr 28;298(2):273-82. doi: 10.1006/jmbi.2000.3671.
PMID: 10764596

Structure of the outer membrane protein A transmembrane domain
Nat Struct Biol. 1998 Nov;5(11):1013-7. doi: 10.1038/2983.
PMID: 9808047

Proteins in this family with 3D-structure
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