P0C940 · FIMA1_PORGN

Function

function

Structural subunit of the major fimbriae (PubMed:1987052).
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 (PubMed:11748193, PubMed:1987052).
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.

138350100150200250300350
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-1
  • Short names
    FimA1
  • Alternative names
    • Fimbrillin (Fimbrilin)
    • Major fimbrial subunit protein type I

Gene names

    • Name
      fimA

Organism names

Accessions

  • Primary accession
    P0C940
  • Secondary accessions
    • P13793
    • Q51821

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 variant247in strain: BH18/10

Variants

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

The viewer provides 1 variant 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_000000915619-46
ChainPRO_000000915747-383Major fimbrium subunit FimA type-1

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
Region374-383Important 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
    383
  • Mass (Da)
    41,367
  • Last updated
    2016-07-06 v2
  • MD5 Checksum
    707457EBE208BF8288E3C5FBFEA072A1
MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW

Sequence caution

The sequence AAA16482.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA04620.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA04622.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict164in Ref. 1; AAA16482

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M19405
EMBL· GenBank· DDBJ
AAA16482.1
EMBL· GenBank· DDBJ
Unassigned DNA Different initiation
D17794
EMBL· GenBank· DDBJ
BAA04620.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
D17796
EMBL· GenBank· DDBJ
BAA04622.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
D42067
EMBL· GenBank· DDBJ
BAA22414.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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