B2RHG1 · MFA1_PORG3

Function

function

Structural subunit of the minor fimbriae (PubMed:12593606, PubMed:19589838, PubMed:24118823).
These 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 (PubMed:11083792, PubMed:12593606, PubMed:15972485, PubMed:19589838, PubMed:23809984, PubMed:24118823, PubMed:26001707, PubMed:26437277).
They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Mfa1 orthologs from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable)

Miscellaneous

The name (minor 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 ATCC BAA-1703 / FDC 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 ATCC BAA-1703 / FDC 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.

TypeIDPosition(s)Description
Site49-50Cleavage; by gingipain

GO annotations

AspectTerm
Cellular Componentcell outer membrane
Cellular Componentouter membrane
Cellular Componentpilus shaft
Biological Processcell-cell adhesion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Minor fimbrium subunit Mfa1
  • Alternative names
    • Pg-II fim a

Gene names

    • Name
      mfa1
    • Ordered locus names
      PGN_0287

Organism names

Accessions

  • Primary accession
    B2RHG1

Proteomes

Subcellular Location

Fimbrium
Cell outer membrane
Note: Probably synthesized as a palmitoylated precursor. Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (Probable).

Keywords

Phenotypes & Variants

Disruption phenotype

Mfa1-deficient cells show increased autoaggregation. Double mutants lacking both FimA and Mfa1 lack major and minor fimbriae; they fail to adhere to host cells.

PTM/Processing

Features

Showing features for signal, lipidation, propeptide, chain.

TypeIDPosition(s)Description
Signal1-19
Lipidation20N-palmitoyl cysteine
Lipidation20S-diacylglycerol cysteine
PropeptidePRO_000043679020-49
ChainPRO_000043679150-563Minor fimbrium subunit Mfa1

Keywords

Interaction

Subunit

Structural component of the fimbrial stalk. Minor fimbriae are composed of a structural subunit, most often Mfa1, and the accessory subunits Mfa3, Mfa4 and Mfa5 (PubMed:19589838, PubMed:24118823, PubMed:26001707, PubMed:26437277).
Mfa1 interacts with Mfa2; this anchors the fimbrium in the membrane (PubMed:19589838).
Fimbrium assembly occurs by linear, head-to-tail oligomerization of fimbrial subunits. This is mediated via insertion of a C-terminal beta-strand from one subunit into a groove in the N-terminal domain of the following subunit (Probable). Interacts with S.gordonii ssp5 (PubMed:11083792, PubMed:15972485).

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region504-543Disordered
Compositional bias506-536Pro residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    563
  • Mass (Da)
    60,786
  • Last updated
    2008-07-01 v1
  • Checksum
    65F205CBDFF5A173
MKLNKMFLVGALLSLGFASCSKEGNGPDPDNAAKSYMSMTLSMPMGSARAGDGQDQANPDYHYVGEWAGKDKIEKVSIYMVPQGGPGLVESAEDLDFGTYYENPTIDPATHNAILKPKKGIKVNSAVGKTVKVYVVLNDIAGKAKALLANVNAADFDAKFKEIIELSTQAQALGTVADGPNPATAAGKIAKKNGTTDETIMMTCLQPSDALTIEAAVSEANAIAGIKNQAKVTVERSVARAMVSTKAQSYEIKATTQIGEIAAGSVLATITDIRWVVAQGERRQYLSKKRGTVPENTWVTPGSGFVPTSSTFHTNATEYYDYAGLWEDHNTNEAVISGTQVPTLADYQLQDVTGELANALSGKFLLPNTHKSGANAASSDYKRGNTAYVLVRAKFTPKKEAFIDRGKTYSDNTAVPEYVAGEDFFVGENGQFYVSMKSVTDPKVGGVAGMKAHKYVKGKVLYYAWLNPSTTSPDSWWNSPVVRNNIYHIHIKSIKKLGFNWNPLVPDPDPSNPENPNNPDPNPDEPGTPVPTDPENPLPDQDTFMSVEVTVLPWKVHSYEVDL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias506-536Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009380
EMBL· GenBank· DDBJ
BAG32806.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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