Summary: Autotransporter beta-domain
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "Autotransporter domain". More...
Autotransporter domain
| Structure of the translocator domain of a bacterial autotransporter.[1] | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Autotransporter | ||||||||
| Pfam | PF03797 | ||||||||
| InterPro | IPR005546 | ||||||||
| PROSITE | PDOC51208 | ||||||||
| SCOP | 1uyn | ||||||||
| SUPERFAMILY | 1uyn | ||||||||
| TCDB | 1.B.12 | ||||||||
| OPM superfamily | 28 | ||||||||
| OPM protein | 1uyo | ||||||||
|
|||||||||
In molecular biology an autotransporter domain is a structural domain found in some outer membrane proteins.
Translocation of polypeptide chains through the outer membrane of Gram-negative bacteria is termed secretion. Secretion occurs via a number of different pathways in this type of bacterium. One of these pathways, known as the type V(a) secretion pathway is exemplified by the prototypical IgA1 Protease of Neisseria gonorrhoeae [2]. In fact 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 from Gram-negative bacteria.
The protein domain shown to be absolutely necessary to mediate secretion through the outer membrane is contained within the C-terminal portion of the translated protein itself, which undergoes post-translational modification prior to secretion of a passenger domain, hence proteins secreted in this way are called autotransporters. 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, and may or may not remain associated with, the translocator domain[3]. In those proteins where the cleavage is auto-catalytic, the peptidase domains belong to MEROPS peptidase families S6 and S8. Passenger domains structurally characterised to date have been shown to be dominated by a protein fold known as a beta helix, the folding of which is thought to be intrinsically linked to its method of outer membrane translocation.
[edit] References
- ^ Oomen, C. J.; Van Ulsen, P.; Van Gelder, P.; Feijen, M.; Tommassen, J.; Gros, P. (2004). "Structure of the translocator domain of a bacterial autotransporter". The EMBO Journal 23 (6): 1257–1266. doi:10.1038/sj.emboj.7600148. PMC 381419. PMID 15014442. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=381419.
- ^ Pohlner, J.; Halter, R.; Beyreuther, K.; Meyer, T. F. (1987). "Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease". Nature 325 (6103): 458–462. doi:10.1038/325458a0. PMID 3027577.
- ^ Henderson, I. R.; Navarro-Garcia, F.; Nataro, J. P. (1998). "The great escape: Structure and function of the autotransporter proteins". Trends in microbiology 6 (9): 370–378. PMID 9778731.
[edit] Further reading
- Veiga, E.; Sugawara, E.; Nikaido, H.; De Lorenzo, V.; Fernández, L. A. (2002). "Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains". The EMBO Journal 21 (9): 2122–2131. doi:10.1093/emboj/21.9.2122. PMC 125980. PMID 11980709. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125980.
- Oomen, C. J.; Van Ulsen, P.; Van Gelder, P.; Feijen, M.; Tommassen, J.; Gros, P. (2004). "Structure of the translocator domain of a bacterial autotransporter". The EMBO Journal 23 (6): 1257–1266. doi:10.1038/sj.emboj.7600148. PMC 381419. PMID 15014442. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=381419.
| This membrane protein-related article is a stub. You can help Wikipedia by expanding it. |
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Autotransporter beta-domain
Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type V pathway was first described for the IgA1 protease [2]. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different protease is used and in some cases no cleavage occurs [1].
Literature references
-
Henderson IR, Navarro-Garcia F, Nataro JP; , Trends Microbiol 1998;6:370-378.: The great escape: structure and function of the autotransporter proteins. PUBMED:9778731
-
Pohlner J, Halter R, Beyreuther K, Meyer TF; , Nature 1987;325:458-462.: Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. PUBMED:3027577
-
Veiga E, Sugawara E, Nikaido H, de Lorenzo V, Fernandez LA; , EMBO J 2002;21:2122-2131.: Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. PUBMED:11980709
-
Oomen CJ, Van Ulsen P, Van Gelder P, Feijen M, Tommassen J, Gros P; , EMBO J 2004;23:1257-1266.: Structure of the translocator domain of a bacterial autotransporter. PUBMED:15014442
Clan
This family is a member of clan MBB (CL0193), which has a total of 51 members.
External database links
| MEROPS: | S8 S6 |
| PANDIT: | PF03797 |
| Pseudofam: | PF03797 |
| SCOP: | 1uyn |
| SYSTERS: | Autotransporter |
| Transporter classification: | 1.B.12 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR005546
Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease [PUBMED:3027577]. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C terminus of the proteins it occurs in. The N terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs [PUBMED:9778731]. In those proteins where the cleavage is auto-catalytic, the peptidase domains belong to MEROPS peptidase families S6 and S8.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Pfam Clan
This family is a member of clan MBB (CL0193), which contains the following 51 members:
Ail_Lom Autotransporter Bac_surface_Ag Campylo_MOMP Channel_Tsx CopB DUF1302 DUF1597 DUF2320 DUF2490 DUF2860 DUF3078 DUF3138 DUF3187 DUF3308 DUF3575 DUF4289 DUF481 DUF560 Gcw_chp HP_OMP HP_OMP_2 KdgM LamB MipA OMP_b-brl OMP_b-brl_2 OmpA_membrane Omptin OmpW Opacity OpcA OprB OprD OprF OstA_C PagL Phenol_MetA_deg Porin_1 Porin_2 Porin_4 Porin_O_P Porin_OmpG ShlB Surface_Ag_2 Toluene_X TonB_dep_Rec TraF_2 TSA Usher YfaZAlignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | [1] |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 212 |
| Number in full: | 4980 |
| Average length of the domain: | 240.70 aa |
| Average identity of full alignment: | 15 % |
| Average coverage of the sequence by the domain: | 25.67 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 265 | ||||||||||||
| Family (HMM) version: | 14 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
HideWeight segments by...
Change the size of the sunburst
Colour assignments
Archea
|
Eukaryota
|
Bacteria
|
Other sequences
|
Viruses
|
Unclassified
|
Viroids
|
Unclassified sequence
|
This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab if you need to select sub-trees and view sequence alignments. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Autotransporter domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence