Summary: Major fimbrial subunit protein (FimA)
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Major fimbrial subunit protein (FimA) Provide feedback
This family consists of several Porphyromonas gingivalis major fimbrial subunit protein (FimA) sequences. Fimbriae of Porphyromonas gingivalis, a periodontopathogen, play an important role in its adhesion to and invasion of host cells. The fimA genes encoding fimbrillin (FimA), a subunit protein of fimbriae, have been classified into five types, types I to V, based on nucleotide sequences. It has been found that type II FimA can bind to epithelial cells most efficiently through specific host receptors . Human dental plaque is a multispecies microbial biofilm that is associated with two common oral diseases, dental caries and periodontal disease. There is an inter-species contact-dependent communication system between P. gingivalis and S. cristatus that involces the Arc-A enzyme .
Nakagawa I, Amano A, Kuboniwa M, Nakamura T, Kawabata S, Hamada S; , Infect Immun 2002;70:277-285.: Functional differences among FimA variants of Porphyromonas gingivalis and their effects on adhesion to and invasion of human epithelial cells. PUBMED:11748193 EPMC:11748193
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008110
Periodontal disease in humans is a major health problem in the developed world, and is caused by a number of specialised pathogens that inhabit the oral cavity. Amongst the bacterial species culturable from periodontal lesions are the streptococcal microbes Streptococcus mutans and Streptococcus sobrinus, and the Gram-negative anaerobe Porphyromonas gingivalis (Bacteroides gingivalis) [PUBMED:2895100]. The latter bacterium has been implicated as the causative agent of peridontitis, pulpal infections and tonsillar abcesses [PUBMED:2895100].
Adherence by P. gingivalis to the periodontal surface is mediated by its major virulence factor fimbriae [PUBMED:1987052]. This differs from other pathogenic Gram-negative bacterial polymeric Type I and IV fimbriae/pili in that it is much more simplified, consisting of only a monomeric fimbrillin repeating subunit, Fma1/FimA. Fma1/FimA has a molecular weight of 43kDa, and can exhibit antigenic diversity in different P. gingivalis strains [PUBMED:1987052]. Unusually, this form of fimbrillin possesses a far longer leader peptide compared to the fimbrial subunits of other bacteria [PUBMED:1987052]. It has been hypothesised that this allows for the maturation of the preprotein during secretion [PUBMED:1987052].
Recently, a study into the different antigenic types of P. gingivalis fimbrillin classified them into five distinct groups, depending on their gene sequences [PUBMED:11748193]. Investigations into the functional differences of each type revealed that in the majority of peridontitis cases, bacterial strains possessing the type II Fma1/FimA were the most prevalent [PUBMED:11748193]; in healthy adults, type I strains were the most common. This has implications for particular strains that are associated with periodontal disease.
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|Molecular function||structural molecule activity (GO:0005198)|
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To add the reference from ActaF when it is published, A conserved fold for fimbriae components revealed by the crystal structure of a putative fimbriae assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Angstrom resolution. This family includes the fimbrillin-A set of fimbrial proteins and the shorter Mfa1 fimbrial set and their asoociated anchor-proteins Mfa2.
The clan contains the following 2 members:Mfa2 P_gingi_FimA
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Curation and family details
|Seed source:||Pfam-B_13339 (release 9.0)|
|Number in seed:||32|
|Number in full:||270|
|Average length of the domain:||299.40 aa|
|Average identity of full alignment:||14 %|
|Average coverage of the sequence by the domain:||54.52 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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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 P_gingi_FimA domain has been found. There are 6 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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