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InterPro: IPR005546 Autotransporter beta-domain

Protein matchesHelp
UniProtKB
Matches:
3395 proteins
AccessionHelp IPR005546 Auto_transptbeta
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR003991 Pertactin virulence factor, C-terminal
Found in IPR006315 Outer membrane autotransporter barrel
IPR016955 Autotransporter, YhjY, predicted
IPR017186 Lipase, autotransporter EstA
IPR017318 Peptidase S8A, subtilisin-related, campylobacter
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 [1]. 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 [2]. In those proteins where the cleavage is auto-catalytic, the peptidase domains belong to MEROPS peptidase families S6 and S8.

Structural linksHelp
SCOP: f.4.5.1
Database linksHelp
PROSITE doc: PDOC51208
PANDIT: PF03797
Blocks: IPB005546
MEROPS: S6 , S8
Pfam Clan: CL0193.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005546 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O32591 Serine protease espP

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005546 Autotransporter beta-domain
IPR012332 Phage P22 tailspike
IPR009003 Serine/cysteine peptidase, trypsin-like
IPR000710 Peptidase S6, IgA endopeptidase
IPR006315 Outer membrane autotransporter barrel
IPR011050 Pectin lyase fold/virulence factor
PDB Chain
ModBase

PublicationsHelp
1. Pohlner J, Halter R, Beyreuther K, Meyer TF.
Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease.
Nature 325 458-62 1987 [PubMed: 3027577]
http://dx.doi.org/10.1038/325458a0
2. Henderson IR, Navarro-Garcia F, Nataro JP.
The great escape: structure and function of the autotransporter proteins.
Trends Microbiol. 6 370-8 1998 [PubMed: 9778731]
http://dx.doi.org/10.1016/S0966-842X(98)01318-3

Additional ReadingHelp
Henderson IR, Navarro-Garcia F, Desvaux M, Fernandez RC, Ala'Aldeen D.
Type V protein secretion pathway: the autotransporter story.
Microbiol. Mol. Biol. Rev. 68 2004 692-744 [PubMed: 15590781]
http://dx.doi.org/10.1128/MMBR.68.4.692-744.2004
Loveless BJ, Saier MH Jr.
A novel family of channel-forming, autotransporting, bacterial virulence factors.
Mol. Membr. Biol. 14 1997 113-23 [PubMed: 9394291]
Oomen CJ, van Ulsen P, van Gelder P, Feijen M, Tommassen J, Gros P.
Structure of the translocator domain of a bacterial autotransporter.
EMBO J. 23 2004 1257-66 [PubMed: 15014442]
http://dx.doi.org/10.1038/sj.emboj.7600148
Veiga E, Sugawara E, Nikaido H, de Lorenzo V, Fernandez LA.
Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains.
EMBO J. 21 2002 2122-31 [PubMed: 11980709]
http://dx.doi.org/10.1093/emboj/21.9.2122
Veiga E, de Lorenzo V, Fernandez LA.
Structural tolerance of bacterial autotransporters for folded passenger protein domains.
Mol. Microbiol. 52 2004 1069-80 [PubMed: 15130125]
http://dx.doi.org/10.1111/j.1365-2958.2004.04014.x
Jacob-Dubuisson F, Fernandez R, Coutte L.
Protein secretion through autotransporter and two-partner pathways.
Biochim. Biophys. Acta 1694 2004 235-57 [PubMed: 15546669]
http://dx.doi.org/10.1016/j.bbamcr.2004.03.008
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InterPro 23.1