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2  structures 168  species 0  interactions 296  sequences 61  architectures

Family: IAT_beta (PF11924)

Summary: Inverse autotransporter, beta-domain

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This is the Wikipedia entry entitled "Intimin". More...

Intimin Edit Wikipedia article

Intimin C-type lectin domain
PDB 1e5u EBI.jpg
nmr representative structure of intimin-190 (int190) from enteropathogenic e. coli
Identifiers
Symbol Intimin_C
Pfam PF07979
Pfam clan CL0056
InterPro IPR013117

Intimin is a virulence factor (adhesin) of EPEC (e.g. E. coli O127:H6) and EHEC (e.g. E. coli O157:H7) E. coli strains. It is an attaching and effacing (A/E) protein which with other virulence factors is responsible for enteropathogenic and enterohaemorrhagic diarrhoea.[1]

Intimin is expressed on the bacterial cell surface where it can bind to its receptor Tir (Translocated intimin receptor). Tir, along with over 25 other bacterial proteins, is secreted from attaching and effacing E. coli directly into the cytoplasm of intestinal epithelial cells by a Type three secretion system. Once within the cytoplasm of the host cell, Tir is inserted into the plasma membrane, allowing surface exposure and intimin binding.[1]

The structure of the C-terminal domain has been solved and shown to have a C-lectin type of structure.[2]

It is a 94 kDa outer membrane protein encoded by eaeA gene in the locus of enterocyte effacement. Mutations in the eaeA gene result in loss of ability to cause A/E lesions, and is required for full virulence in infected volunteers and animal models. The N-terminal domains of intimin from A/E lesion forming pathogens have high homology with each other and to invasin from Yersinia pseudotuberculosis and Yersinia enterocolitica, whereas the C-terminal domains show less homology.

Antibodies to intimin are present in: (1) Immune colostrum from mothers in EPEC endemic areas, (2) The serum of EPEC/EHEC infected children and EPEC infected volunteers, and (3) Secretions of Citrobacter rodentium infected mice.

References

  1. ^ a b Stevens, J.; et al. (2006). "Actin-dependent movement of bacterial pathogens". Nature Reviews Microbiology. 4: 91–101. doi:10.1038/nrmicro1320. PMID 16415925. 
  2. ^ Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S (June 2000). "Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli". EMBO J. 19 (11): 2452–64. doi:10.1093/emboj/19.11.2452. PMC 212744Freely accessible. PMID 10835344. 

[1] This article incorporates text from the public domain Pfam and InterPro IPR013117


  1. ^ Ahmed, S; et al. (2013). "A directed intimin insertion mutant of a rabbit enteropathogenic Escherichia coli (REPEC) is attenuated, immunogenic and elicits serogroup specific protection.". Vet Immunol Immunopathol. 152 (1-2): 146–155. doi:10.1016/j.vetimm.2012.09.035. PMID 23084628. 

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.

Inverse autotransporter, beta-domain Provide feedback

This is a family of beta-barrel porin-like outer membrane proteins from enteropathogenic Gram-negative bacteria. Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They carry C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal beta domains that are embedded in the outer membrane. This family represents the beta-barrel porin-like domain in the outer membrane that can be found in intimins, invasins and some inverse autotransporters [1,2].

Literature references

  1. Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, Buchanan SK;, Structure. 2012;20:1233-1243.: Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. PUBMED:22658748 EPMC:22658748

  2. Leo JC, Oberhettinger P, Schutz M, Linke D;, Int J Med Microbiol. 2015;305:276-282.: The inverse autotransporter family: intimin, invasin and related proteins. PUBMED:25596886 EPMC:25596886


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR024519

This domain is found in a group of beta-barrel porin-like outer membrane proteins from enteropathogenic Gram-negative bacteria. Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They carry C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal beta domains that are embedded in the outer membrane. This entry represents the beta-barrel porin-like domain in the outer membrane that can be found in intimins, invasins and some inverse autotransporters [PUBMED:22658748, PUBMED:25596886].

Intimin is believed to mediate adherence and it is necessary for the production of attaching and effacing lesions on tissue culture cells [PUBMED:2172966]. Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells [PUBMED:3304658]. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins [PUBMED:10514372].

Domain organisation

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Alignments

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  Seed
(38)
Full
(296)
Representative proteomes UniProt
(2935)
NCBI
(7999)
Meta
(539)
RP15
(44)
RP35
(118)
RP55
(281)
RP75
(720)
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  Seed
(38)
Full
(296)
Representative proteomes UniProt
(2935)
NCBI
(7999)
Meta
(539)
RP15
(44)
RP35
(118)
RP55
(281)
RP75
(720)
Alignment:
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  Seed
(38)
Full
(296)
Representative proteomes UniProt
(2935)
NCBI
(7999)
Meta
(539)
RP15
(44)
RP35
(118)
RP55
(281)
RP75
(720)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

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Trees

This page displays the phylogenetic tree for this family's seed alignment. 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 alignment.

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Curation and family details

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Curation View help on the curation process

Seed source: PFAM-B_890 (release 23.0)
Previous IDs: DUF3442; Invasin_beta;
Type: Domain
Author: Assefa S, Coggill PC, Bateman A
Number in seed: 38
Number in full: 296
Average length of the domain: 241.60 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 29.58 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.4 21.4
Noise cut-off 20.9 20.7
Model length: 276
Family (HMM) version: 7
Download: download the raw HMM for this family

Species distribution

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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 IAT_beta domain has been found. There are 2 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.

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