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0  structures 26  species 0  interactions 31  sequences 2  architectures

Family: Ail_Lom (PF06316)

Summary: Enterobacterial Ail/Lom protein

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Enterobacterial Ail/Lom protein Provide feedback

This family consists of several bacterial and phage Ail/Lom-like proteins. The Yersinia enterocolitica Ail protein is a known virulence factor. Proteins in this family are predicted to consist of eight transmembrane beta-sheets and four cell surface-exposed loops. It is thought that Ail directly promotes invasion and loop 2 contains an active site, perhaps a receptor-binding domain [1]. The phage protein Lom is expressed during lysogeny, and encode host-cell envelope proteins. Lom is found in the bacterial outer membrane, and is homologous to virulence proteins of two other enterobacterial genera. It has been suggested that lysogeny may generally have a role in bacterial survival in animal hosts, and perhaps in pathogenesis [2].

Literature references

  1. Miller VL, Beer KB, Heusipp G, Young BM, Wachtel MR; , Mol Microbiol 2001;41:1053-1062.: Identification of regions of Ail required for the invasion and serum resistance phenotypes. PUBMED:11555286 EPMC:11555286

  2. Barondess JJ, Beckwith J; , Nature 1990;346:871-874.: A bacterial virulence determinant encoded by lysogenic coliphage lambda. PUBMED:2144037 EPMC:2144037


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000758

Virulence-related outer membrane proteins are expressed in Gram-negative bacteria and are essential to bacterial survival within macrophages and for eukaryotic cell invasion. Members of this group include:
  • PagC, required by Salmonella typhimurium for survival in macrophages and for virulence in mice [PUBMED:1766380]
  • Rck outer membrane protein of the S. typhimurium virulence plasmid [PUBMED:8675302]
  • Ail, a product of the Yersinia enterocolitica chromosome capable of mediating bacterial adherence to and invasion of epithelial cell lines [PUBMED:1688838]
  • OmpX from Escherichia coli that promotes adhesion to and entry into mammalian cells. It also has a role in the resistance against attack by the human complement system [PUBMED:1987115]
  • a Bacteriophage lambda outer membrane protein, Lom [PUBMED:1846140]
  • The crystal structure of OmpX from E. coli reveals that OmpX consists of an eight-stranded antiparallel all-next-neighbour beta barrel [PUBMED:10545325]. The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior. The core of the barrel consists of an extended hydrogen-bonding network of highly conserved residues. OmpX thus resembles an inverse micelle. The OmpX structure shows that the membrane-spanning part of the protein is much better conserved than the extracellular loops. Moreover, these loops form a protruding beta sheet, the edge of which presumably binds to external proteins. It is suggested that this type of binding promotes cell adhesion and invasion and helps defend against the complement system. Although OmpX has the same beta-sheet topology as the structurally related outer membrane protein A (OmpA) INTERPRO, their barrels differ with respect to the shear numbers and internal hydrogen-bonding networks.

    Gene Ontology

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    Domain organisation

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    Alignments

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      Seed
    (2)
    Full
    (31)
    Representative proteomes UniProt
    (1617)
    NCBI
    (5638)
    Meta
    (2)
    RP15
    (5)
    RP35
    (15)
    RP55
    (40)
    RP75
    (211)
    Alignment:
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      Seed
    (2)
    Full
    (31)
    Representative proteomes UniProt
    (1617)
    NCBI
    (5638)
    Meta
    (2)
    RP15
    (5)
    RP35
    (15)
    RP55
    (40)
    RP75
    (211)
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    Curation and family details

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    Curation View help on the curation process

    Seed source: Pfam-B_12325 (release 9.0)
    Previous IDs: none
    Type: Family
    Author: Moxon SJ
    Number in seed: 2
    Number in full: 31
    Average length of the domain: 173.80 aa
    Average identity of full alignment: 32 %
    Average coverage of the sequence by the domain: 97.50 %

    HMM information View help on HMM parameters

    HMM build commands:
    build method: hmmbuild -o /dev/null HMM SEED
    search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
    Model details:
    Parameter Sequence Domain
    Gathering cut-off 20.8 20.8
    Trusted cut-off 21.7 22.4
    Noise cut-off 20.5 20.7
    Model length: 199
    Family (HMM) version: 9
    Download: download the raw HMM for this family

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