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The YadA-like membrane anchor domain (Autotransporter-2) Family [Function: Biogenesis/Secretion] Seed alignment | Full alignment | Pfam page | TC-DB page

The type V secretion pathway encompasses the autotransporter proteins (AT-1), the two-partner secretion system (TPS) and the recently described type AT-2 family of proteins. The prototype of the last family is the adhesin A (YadA) of Yersinia enterocolitica. Homologs are found in a variety of pathogenic bacteria. Proteins of this family mediate attachment to the surfaces of host cells and protect bacteria against complement and the bactericidal activities of defensins. Adhesins of this family form oligomeric lollipop-like structures anchored in the outer membrane by their C-termini. In contrast to the typical autotransporters, whose C-terminal porin regions are of about 250 residues long and possess 12 transmembrane ß strands, members of the AT-2 family, have their C-terminal pore-forming anchors composed of about only 70 residues, with just 4 possible transmembrane ß strands and form trimers. These facts suggest that the pore-forming translocator units evolved independently and they belong to distinct families. The structure of one such protein, the HiA autotransporter of Haemophilus influenzae has been solved revealing a ß-barrel with 12 transmembrane ß-strands, comprised by 4 strands from each subunit. The central channel has a pore of 1.8 nm in diameter that is traversed by three N-terminal alpha helices, one from each subunit.

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Literature references

Biogenesis and function of the autotransporter adhesins YadA, intimin and invasin
Int J Med Microbiol. 2019 Jul;309(5):331-337. doi: 10.1016/j.ijmm.2019.05.009. Epub 2019 Jun 1.
PMID: 31176600

In vitro assembly of Haemophilus influenzae adhesin transmembrane domain and studies on the electrostatic repulsion at the interface
Biophys Rev. 2019 Jun;11(3):303-309. doi: 10.1007/s12551-019-00535-0. Epub 2019 May 9.
PMID: 31073957

Electrostatic Repulsion between Unique Arginine Residues Is Essential for the Efficient in Vitro Assembly of the Transmembrane Domain of a Trimeric Autotransporter
Biochemistry. 2017 Apr 18;56(15):2139-2148. doi: 10.1021/acs.biochem.6b01130. Epub 2017 Apr 10.
PMID: 28357859

Yeast Mitochondria as a Model System to Study the Biogenesis of Bacterial ß-Barrel Proteins
Methods Mol Biol. 2015;1329:17-31. doi: 10.1007/978-1-4939-2871-2_2.
PMID: 26427673

Yersinia adhesin A (YadA)--beauty & beast
Int J Med Microbiol. 2015 Feb;305(2):252-8. doi: 10.1016/j.ijmm.2014.12.008. Epub 2014 Dec 24.
PMID: 25604505

Evolutionary conservation in biogenesis of ß-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein
J Biol Chem. 2014 Oct 24;289(43):29457-70. doi: 10.1074/jbc.M114.565655. Epub 2014 Sep 4.
PMID: 25190806

Yersinia infection tools-characterization of structure and function of adhesins
Front Cell Infect Microbiol. 2013 Jan 8;2:169. doi: 10.3389/fcimb.2012.00169. eCollection 2012.
PMID: 23316485

Stability and membrane interactions of an autotransport protein: MD simulations of the Hia translocator domain in a complex membrane environment
Biochim Biophys Acta. 2013 Feb;1828(2):715-23. doi: 10.1016/j.bbamem.2012.09.002. Epub 2012 Sep 13.
PMID: 22982599

The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation
J Bacteriol. 2012 Feb;194(4):827-38. doi: 10.1128/JB.05322-11. Epub 2011 Dec 9.
PMID: 22155776

Mitochondria can recognize and assemble fragments of a beta-barrel structure
Mol Biol Cell. 2011 May 15;22(10):1638-47. doi: 10.1091/mbc.E10-12-0943. Epub 2011 Apr 1.
PMID: 21460184

Structure and biology of trimeric autotransporter adhesins
Adv Exp Med Biol. 2011;715:143-58. doi: 10.1007/978-94-007-0940-9_9.
PMID: 21557062

Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
EMBO J. 2006 Jun 7;25(11):2297-304. doi: 10.1038/sj.emboj.7601132. Epub 2006 May 11.
PMID: 16688217

The Haemophilus influenzae Hia autotransporter contains an unusually short trimeric translocator domain
J Biol Chem. 2004 Apr 9;279(15):14679-85. doi: 10.1074/jbc.M311496200. Epub 2004 Jan 15.
PMID: 14726537

Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesin YadA
J Bacteriol. 2003 Jul;185(13):3735-44. doi: 10.1128/jb.185.13.3735-3744.2003.
PMID: 12813066

YadA, the multifaceted Yersinia adhesin
Int J Med Microbiol. 2001 Aug;291(3):209-18. doi: 10.1078/1438-4221-00119.
PMID: 11554561

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