B2RHG1 · MFA1_PORG3
- ProteinMinor fimbrium subunit Mfa1
- Genemfa1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids563 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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)
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 49-50 | Cleavage; by gingipain | ||||
Sequence: RA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Cellular Component | outer membrane | |
Cellular Component | pilus shaft | |
Biological Process | cell-cell adhesion |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMinor fimbrium subunit Mfa1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Porphyromonadaceae > Porphyromonas
Accessions
- Primary accessionB2RHG1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKLNKMFLVGALLSLGFAS | ||||||
Lipidation | 20 | N-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 20 | S-diacylglycerol cysteine | ||||
Sequence: C | ||||||
Propeptide | PRO_0000436790 | 20-49 | ||||
Sequence: CSKEGNGPDPDNAAKSYMSMTLSMPMGSAR | ||||||
Chain | PRO_0000436791 | 50-563 | Minor fimbrium subunit Mfa1 | |||
Sequence: AGDGQDQANPDYHYVGEWAGKDKIEKVSIYMVPQGGPGLVESAEDLDFGTYYENPTIDPATHNAILKPKKGIKVNSAVGKTVKVYVVLNDIAGKAKALLANVNAADFDAKFKEIIELSTQAQALGTVADGPNPATAAGKIAKKNGTTDETIMMTCLQPSDALTIEAAVSEANAIAGIKNQAKVTVERSVARAMVSTKAQSYEIKATTQIGEIAAGSVLATITDIRWVVAQGERRQYLSKKRGTVPENTWVTPGSGFVPTSSTFHTNATEYYDYAGLWEDHNTNEAVISGTQVPTLADYQLQDVTGELANALSGKFLLPNTHKSGANAASSDYKRGNTAYVLVRAKFTPKKEAFIDRGKTYSDNTAVPEYVAGEDFFVGENGQFYVSMKSVTDPKVGGVAGMKAHKYVKGKVLYYAWLNPSTTSPDSWWNSPVVRNNIYHIHIKSIKKLGFNWNPLVPDPDPSNPENPNNPDPNPDEPGTPVPTDPENPLPDQDTFMSVEVTVLPWKVHSYEVDL |
Keywords
- PTM
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).
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).
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 504-543 | Disordered | ||||
Sequence: LVPDPDPSNPENPNNPDPNPDEPGTPVPTDPENPLPDQDT | ||||||
Compositional bias | 506-536 | Pro residues | ||||
Sequence: PDPDPSNPENPNNPDPNPDEPGTPVPTDPEN |
Sequence similarities
Belongs to the bacteroidetes fimbrillin superfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length563
- Mass (Da)60,786
- Last updated2008-07-01 v1
- Checksum65F205CBDFF5A173
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 506-536 | Pro residues | ||||
Sequence: PDPDPSNPENPNNPDPNPDEPGTPVPTDPEN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP009380 EMBL· GenBank· DDBJ | BAG32806.1 EMBL· GenBank· DDBJ | Genomic DNA |