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Protein

Major fimbrial subunit protein type-3

Gene

fimA

Organism
Porphyromonas gingivalis
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Fimbrillin is the structural subunit of the fimbriae, that are filamentous appendages on the cell surface. Fimbriae of P.gingivalis are recognized as a major virulence factor as they mediate cell adhesion and play an important role in invasion of periodontal tissues.1 Publication

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Major fimbrial subunit protein 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

GO - Cellular componenti

  1. pilus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Fimbrium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1010By similarityPRO_0000009164
Chaini11 – 353343Major fimbrial subunit protein type-3PRO_0000009165Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the P.gingivalis fimbrillin family.Curated

Family and domain databases

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

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
MVLKTSNPNR AFGNAGDEAK VAKLTVMVYK GEQQEAIKSV ENAIKVENIK
60 70 80 90 100
CGAGQRTLVV MANTGGMELA GKTLAEVKAL TTELTEGNQE AAGLIMTAEP
110 120 130 140 150
VEVTLVAGNN YYGYDGSQGG NQISQGTPLE IKRVHARIAF TKIEVTMSQS
160 170 180 190 200
YANKYNFAPE NIYALVAKKK SNLFGASLAN SDDAYLTGSL TTFNGAYSPA
210 220 230 240 250
NYTHVDWLGR DYTEIGAATV NTPKGFYVLE STYAQNAGLR PTILCVKGKL
260 270 280 290 300
TKHDGTALSS EEMTAAFNAG WIVANNDPTT YYPVLVNFES NNYTYTGEAV
310 320 330 340 350
EKGKIVRNHK FDINLTITGP GTNNPENPIT ESANLNVNCV VAAWKGVVQN

VIW
Length:353
Mass (Da):38,024
Last modified:October 31, 1996 - v1
Checksum:i7FBE4FBF427EA2AB
GO

Sequence databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17801 Genomic DNA. Translation: BAA04627.1.
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.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and sequencing of the fimbrilin gene of Porphyromonas gingivalis strains and characterization of recombinant proteins."
    Fujiwara T., Morishima S., Takahashi I., Hamada S.
    Biochem. Biophys. Res. Commun. 197:241-247(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 6/26.
  2. "Functional differences among FimA variants of Porphyromonas gingivalis and their effects on adhesion to and invasion of human epithelial cells."
    Nakagawa I., Amano A., Kuboniwa M., Nakamura T., Kawabata S., Hamada S.
    Infect. Immun. 70:277-285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CLASSIFICATION INTO TYPES.

Entry informationi

Entry nameiFIMA3_PORGN
AccessioniPrimary (citable) accession number: Q51826
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2002
Last sequence update: October 31, 1996
Last modified: January 6, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.