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 IPR029141
This entry represents the N-terminal of the major fimbrial subunit protein (FimA). FimA is the structural subunit of the fimbriae, which are filamentous appendages on the cell surface. Fimbriae of P.gingivalis are recognied as a major virulence factor as they mediate cell adhesion and play an important role in invasion of periodontal tissues [PUBMED:17081195]. FimA proteins 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 [PUBMED:11748193].
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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 5 members:DUF4906 Mfa2 Mfa_like_1 Mfa_like_2 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:||1010|
|Average length of the domain:||300.30 aa|
|Average identity of full alignment:||15 %|
|Average coverage of the sequence by the domain:||55.63 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 10 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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