Q51822 · FIMA2_PORGN
- ProteinMajor fimbrium subunit FimA type-2
- GenefimA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids384 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 46-47 | Cleavage; by gingipain | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Cellular Component | pilus | |
Molecular Function | structural molecule activity | |
Biological Process | cell adhesion |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameMajor fimbrium subunit FimA type-2
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Porphyromonadaceae > Porphyromonas
Accessions
- Primary accessionQ51822
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Note: Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | 100-104 | in strain: OMZ409 | |||
Natural variant | 126 | in strain: OMZ409 | |||
Natural variant | 136 | in 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.
PTM/Processing
Features
Showing features for signal, lipidation, propeptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-18 | ||||
Lipidation | 19 | N-palmitoyl cysteine | |||
Lipidation | 19 | S-diacylglycerol cysteine | |||
Propeptide | PRO_0000009160 | 19-46 | |||
Chain | PRO_0000009161 | 47-384 | Major 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
- PTM
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).
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 375-384 | Important for oligomerization and fimbrium assembly | |||
Sequence similarities
Belongs to the bacteroidetes fimbrillin superfamily. FimA/Mfa1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length384
- Mass (Da)41,869
- Last updated2016-07-06 v2
- Checksum3CB4EFC46E842F5A
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |