Structure of the autotransporter domain NalP from Neisseria meningitidis. PDB entry 1uyn[1]
Identifiers
Symbol
Autotransporter
Pfam
PF03797
InterPro
IPR005546
PROSITE
PDOC51208
SCOP2
1uyn / SCOPe / SUPFAM
TCDB
1.B.12
OPM superfamily
28
OPM protein
1uyo
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
PDB
1uyoX:810-1074 1uynX:810-1074
In molecular biology, an autotransporter domain is a structural domain found in some bacterial outer membrane proteins. The domain is always located at the C-terminal end of the protein and forms a beta-barrel structure. The barrel is oriented in the membrane such that the N-terminal portion of the protein, termed the passenger domain, is presented on the cell surface. These proteins are typically virulence factors, associated with infection or virulence in pathogenic bacteria.
The name autotransporter derives from an initial understanding that the protein was self-sufficient in transporting the passenger domain through the outermembrane. This view has since been challenged by Benz and Schmidt.[2]
Secretion of polypeptide chains through the outer membrane of Gram-negative bacteria can occur via a number of different pathways. The type V(a), or autotransporter, secretion pathway constitutes the largest number of secreted virulence factors of any one of the seven known types of secretion in Gram-negative bacteria. This secretion pathway is exemplified by the prototypical IgA1 Protease of Neisseria gonorrhoeae.[3] The protein is directed to the inner membrane by a signal peptide transported across the inner membrane via the Sec machinery. Once in the periplasm, the autotransporter domain inserts into the outer membrane. The passenger domain is passed through the center of the autotransporter domain to be presented on the outside of the cell, however the mechanism by which this occurs remains unclear.[4]
The C-terminal translocator domain corresponds to an outer membrane beta-barrel domain. The N-terminal passenger domain is translocated across the membrane, and may or may not be cleaved from the translocator domain.[5] In those proteins where the cleavage is auto-catalytic, the peptidase domains belong to MEROPS peptidase families S6 and S8. Passenger domains structurally characterized to date have been shown to be dominated by a protein fold known as a beta helix, typified by pertactin. The folding of this domain is thought to be intrinsically linked to its method of outer membrane translocation.
^Oomen CJ, van Ulsen P, van Gelder P, Feijen M, Tommassen J, Gros P (March 2004). "Structure of the translocator domain of a bacterial autotransporter". The EMBO Journal. 23 (6): 1257–66. doi:10.1038/sj.emboj.7600148. PMC 381419. PMID 15014442.
^Benz I, Schmidt MA (August 2011). "Structures and functions of autotransporter proteins in microbial pathogens". International Journal of Medical Microbiology. 301 (6): 461–8. doi:10.1016/j.ijmm.2011.03.003. PMID 21616712.
^Pohlner J, Halter R, Beyreuther K, Meyer TF (1987). "Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease". Nature. 325 (6103): 458–62. doi:10.1038/325458a0. PMID 3027577. S2CID 25569.
^Leo JC, Grin I, Linke D (April 2012). "Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 367 (1592): 1088–101. doi:10.1098/rstb.2011.0208. PMC 3297439. PMID 22411980.
^Henderson IR, Navarro-Garcia F, Nataro JP (September 1998). "The great escape: structure and function of the autotransporter proteins". Trends in Microbiology. 6 (9): 370–8. doi:10.1016/s0966-842x(98)01318-3. PMID 9778731.
and 23 Related for: Autotransporter family information
In molecular biology, an autotransporter domain is a structural domain found in some bacterial outer membrane proteins. The domain is always located at...
the autotransporters gave rise to the porins which form similar beta-barrel structures.[citation needed] A common example of an autotransporter that...
In molecular biology, trimeric autotransporter adhesins (TAAs), are proteins found on the outer membrane of Gram-negative bacteria. Bacteria use TAAs...
of the crystal structure of the self-cleaving precursor of the Tsh autotransporter from E. coli. These enzymes are synthesized as precursors or propeptides...
infection of the host cell by sticking to the host cell using trimeric autotransporter adhesins. Moraxella catarrhalis is a human pathogen with an affinity...
facilitated by Hap𝘴 autotransporters in the cell wall binding with unknown receptors within the epithelium. The Hap𝘴 autotransporters also facilitate the...
adhesion (Oca). The Oca protein families are a subset of autotransporters, also known as the type Vc or trimeric autotransporters. Trimerization is thought...
humans. It infects the host cell by sticking to it using trimeric autotransporter adhesins. In the United States, about 20,000 cases are diagnosed each...
inside the host cell. For instance, the IcsA effector protein (an autotransporter, not a type-III secretion-system effector) triggers actin reorganization...
for antibody-mediation of pathogen adhesion. Fungal adhesin Trimeric autotransporter adhesins (TAA) Coutte L, Alonso S, Reveneau N, Willery E, Quatannens...
pseudotuberculosis (InvD) is classified under the invasin (InvA)-type autotransporter proteins, yet its structure and function remain undiscovered. This...
activity, they are also called the autotransporter systems. When the secreted proteins are exposed outside, the autotransporters are cut off (cleaved), releasing...
bacterium infects the host by sticking to its cells using trimeric autotransporter adhesins. Y. enterocolitica is widespread in nature, occurring in reservoirs...
A deacylase PagL Opacity family porins (NspA) Autotransporter domain (n=12,S=14) FadL outer membrane protein transport family, including Fatty acid transporter...
Nataro JP (March 2014). "Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence". Cellular...
discovery and description of a new family of secreted proteins: the autotransporters. The name ‘autotransporters’ was first time mentioned in his publication...
invasion. Both rOmpA and rOmpB are members of a family of surface cell antigens (Sca) which are autotransporter proteins; they act as ligands for the Omp proteins...
CCT (TC# 1.C.57)) contain repeat sequences that are also found in autotransporters (e.g., 1.B.12.10.1 and 1.B.40.1.2) as well as TolA (2.C.1.2.1). These...
porin (FUP) family 1.B.12 Autotransporter-1 (AT-1) family 1.B.13 Alginate export porin (AEP) family 1.B.14 Outer membrane receptor (OMR) family 1.B.15 Raffinose...
IV secretion systems, as well as the chaperone/usher pathway, the autotransporter pathway/type V secretion system, and the type VI secretion system (some...
K.; Choi, M.S.; Kim, I.S.; Cho, N.H. (2015). "Immunization with an autotransporter protein of Orientia tsutsugamushi provides protective immunity against...
attachment include pili, filamentous hemagglutinin, fimbriae, protein autotransporters, outer membrane proteins such as pertactin, and other lipopolysaccharide...
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