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Q51826

- FIMA3_PORGN

UniProt

Q51826 - FIMA3_PORGN

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Protein

Major fimbrial subunit protein type-3

Gene
fimA
Organism
Porphyromonas gingivalis
Status
Reviewed - Annotation score: 3 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 – 1010 By similarityPRO_0000009164
Chaini11 – 353343Major fimbrial subunit protein type-3PRO_0000009165Add
BLAST

Family & Domainsi

Sequence similaritiesi

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

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MVLKTSNPNR AFGNAGDEAK VAKLTVMVYK GEQQEAIKSV ENAIKVENIK    50
CGAGQRTLVV MANTGGMELA GKTLAEVKAL TTELTEGNQE AAGLIMTAEP 100
VEVTLVAGNN YYGYDGSQGG NQISQGTPLE IKRVHARIAF TKIEVTMSQS 150
YANKYNFAPE NIYALVAKKK SNLFGASLAN SDDAYLTGSL TTFNGAYSPA 200
NYTHVDWLGR DYTEIGAATV NTPKGFYVLE STYAQNAGLR PTILCVKGKL 250
TKHDGTALSS EEMTAAFNAG WIVANNDPTT YYPVLVNFES NNYTYTGEAV 300
EKGKIVRNHK FDINLTITGP GTNNPENPIT ESANLNVNCV VAAWKGVVQN 350
VIW 353
Length:353
Mass (Da):38,024
Last modified:November 1, 1996 - v1
Checksum:i7FBE4FBF427EA2AB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D17801 Genomic DNA. Translation: BAA04627.1.
PIRiD60275.
JN0920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D17801 Genomic DNA. Translation: BAA04627.1 .
PIRi D60275.
JN0920.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR029141. FimA_N.
IPR008110. Fimbrillin.
[Graphical view ]
Pfami PF06321. P_gingi_FimA. 1 hit.
[Graphical view ]
PRINTSi PR01737. FIMBRILLIN.
ProtoNeti Search...

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(1993) [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(2002) [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 2, 2002
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 59 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

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