Q51822 · FIMA2_PORGN

Function

function

Structural subunit of the major fimbriae (Probable). These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity.

Miscellaneous

The name (major fimbrium subunit) does not indicate the abundance of the protein, but is derived from the greater length of the major fimbriae. In strain ATCC 33277 and strain 381, major fimbriae are 300 - 1600 nM in length and about 5 nm in diameter. In contrast, minor fimbriae are only about 80 - 120 nm long. This length difference is observed only in a small number of strains, including strain ATCC 33277 and strain 381, and is due to a loss of function mutation in FimB, a protein that restricts fimbrial length in other strains.

Features

Showing features for site.

138450100150200250300350
TypeIDPosition(s)Description
Site46-47Cleavage; by gingipain

GO annotations

AspectTerm
Cellular Componentcell outer membrane
Cellular Componentpilus
Molecular Functionstructural molecule activity
Biological Processcell adhesion

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Major fimbrium subunit FimA type-2
  • Alternative names
    • Fimbrillin (Fimbrilin)
    • Major fimbrial subunit protein type II

Gene names

    • Name
      fimA

Organism names

Accessions

  • Primary accession
    Q51822
  • Secondary accessions
    • Q51823
    • Q51824

Subcellular Location

Fimbrium
Cell outer membrane
Note: Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein.

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant100-104in strain: OMZ409
Natural variant126in strain: OMZ409
Natural variant136in strain: OMZ409

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, lipidation, propeptide, chain.

Type
IDPosition(s)Description
Signal1-18
Lipidation19N-palmitoyl cysteine
Lipidation19S-diacylglycerol cysteine
PropeptidePRO_000000916019-46
ChainPRO_000000916147-384Major fimbrium subunit FimA type-2

Post-translational modification

Synthesized as palmitoylated lipoprotein precursor. Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide.

Keywords

Interaction

Subunit

Fimbriae are composed of a major, structural subunit (FimA) and the minor components FimC, FimD and FimE (By similarity).
Head-to-tail oligomerization of FimA molecules mediates assembly of the fimbrium stalk, while the minor components probably form the fimbrium tip. Linear, head-to-tail oligomerization of FimA is mediated by a conformation change, facilitating the insertion of a C-terminal beta-strand into a groove in the N-terminal domain of the following subunit (By similarity).

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region375-384Important for oligomerization and fimbrium assembly

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    384
  • Mass (Da)
    41,869
  • Last updated
    2016-07-06 v2
  • Checksum
    3CB4EFC46E842F5A
MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNPNRAFGEDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGEMKLAGKTLAEVKALTTELTAENQEAAGLIMTAEPVEVTLVAGNNYYGYDGSQGGNQISQDTPLEIKRVHARMAFTEIKVQMSPSYVNKYNFAPENIYALVAKKESNLFGASLANSDDAYLTGSLTNFNGAYSPANYTHVDWLGRDYTEPSNNAPQGFYVLESTYAQNAGLRPTILCVKGKLTKHDGTPLSSEEMTAAFNAGWIVADNNPTTYYPVLVNFNSNNYTYDNGYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW

Sequence caution

The sequence BAA04623.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA04624.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA04625.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D17797
EMBL· GenBank· DDBJ
BAA04623.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
D17798
EMBL· GenBank· DDBJ
BAA04624.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
D17799
EMBL· GenBank· DDBJ
BAA04625.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Similar Proteins

Disclaimer

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