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Protein

Major fimbrium subunit FimA type-3

Gene

fimA

Organism
Porphyromonas gingivalis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.Curated1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Major fimbrium subunit FimA type-3
Alternative name(s):
Fimbrillin
Short name:
Fimbrilin
Major fimbrial subunit protein type III
Gene namesi
Name:fimA
OrganismiPorphyromonas gingivalis
Taxonomic identifieri837 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Subcellular locationi

  • Fimbrium By similarity
  • Cell outer membrane By similarity

  • Note: Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Fimbrium, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818PROSITE-ProRule annotationAdd
BLAST
Propeptidei19 – 4628By similarityPRO_0000009164Add
BLAST
Chaini47 – 389343Major fimbrium subunit FimA type-3PRO_0000009165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi19 – 191N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi19 – 191S-diacylglycerol cysteinePROSITE-ProRule annotation

Post-translational modificationi

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 472Cleavage; by gingipainBy similarity

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

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).By similarity

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni380 – 38910Important for oligomerization and fimbrium assemblyBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR029141. FimA_N.
IPR008110. Fimbrillin.
[Graphical view]
PfamiPF06321. P_gingi_FimA. 1 hit.
[Graphical view]
PRINTSiPR01737. FIMBRILLIN.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q51826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTKFFLLG LAALAMTACN KDNEAEPVTE SNATISVVLK TSNPNRAFGN
60 70 80 90 100
AGDEAKVAKL TVMVYKGEQQ EAIKSVENAI KVENIKCGAG QRTLVVMANT
110 120 130 140 150
GGMELAGKTL AEVKALTTEL TEGNQEAAGL IMTAEPVEVT LVAGNNYYGY
160 170 180 190 200
DGSQGGNQIS QGTPLEIKRV HARIAFTKIE VTMSQSYANK YNFAPENIYA
210 220 230 240 250
LVAKKKSNLF GASLANSDDA YLTGSLTTFN GAYSPANYTH VDWLGRDYTE
260 270 280 290 300
IGAATVNTPK GFYVLESTYA QNAGLRPTIL CVKGKLTKHD GTALSSEEMT
310 320 330 340 350
AAFNAGWIVA NNDPTTYYPV LVNFESNNYT YTGEAVEKGK IVRNHKFDIN
360 370 380
LTITGPGTNN PENPITESAN LNVNCVVAAW KGVVQNVIW
Length:389
Mass (Da):41,833
Last modified:July 6, 2016 - v2
Checksum:i60D39322589614DD
GO

Sequence cautioni

The sequence BAA04627 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17801 Genomic DNA. Translation: BAA04627.1. Different initiation.
PIRiD60275.
JN0920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17801 Genomic DNA. Translation: BAA04627.1. Different initiation.
PIRiD60275.
JN0920.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR029141. FimA_N.
IPR008110. Fimbrillin.
[Graphical view]
PfamiPF06321. P_gingi_FimA. 1 hit.
[Graphical view]
PRINTSiPR01737. FIMBRILLIN.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFIMA3_PORGN
AccessioniPrimary (citable) accession number: Q51826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 6, 2016
Last modified: September 7, 2016
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.Curated

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.