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Protein

Putative fimbrium tip subunit Fim1F

Gene

BDI_3522

Organism
Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Putative component of the fimbrium tip. Fimbriae are filamentous appendages on the cell surface that mediate cell adhesion and biofilm formation.1 Publication

Enzyme and pathway databases

BioCyciPDIS435591:GCNH-3516-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative fimbrium tip subunit Fim1F
Gene namesi
Ordered Locus Names:BDI_3522Imported
OrganismiParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)Imported
Taxonomic identifieri435591 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeParabacteroides
Proteomesi
  • UP000000566 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Fimbrium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 50261 PublicationPRO_0000436738Add
BLAST
Chaini51 – 318268Putative fimbrium tip subunit Fim1FPRO_5002698948Add
BLAST

Interactioni

Subunit structurei

May be part of the fimbrial tip.1 Publication

Protein-protein interaction databases

STRINGi435591.BDI_3522.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R4RX-ray2.38A/B24-318[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA6LHQ9.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OrthoDBiPOG091H15ZL.

Family and domain databases

InterProiIPR029141. FimA_N.
[Graphical view]
PfamiPF06321. P_gingi_FimA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A6LHQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFNVVLFML IVALLGGLST CSSEVPIGFD TDELSFDMSL VLLTGDMQTK
60 70 80 90 100
ASDPNYTYAT TEELTIQNCH VAVFDKDGKR IYFKNFYSKD LGEMKTIGNL
110 120 130 140 150
SGYELQLEGV RTFGKEDKKV SVLVVANANN ANNSPFDNLT TYDGVDNSYT
160 170 180 190 200
AKTIAKGPVT ASLLVKIGKS ETTLKYNQDN APVTVSLIQL SAKIEYTGVY
210 220 230 240 250
KKENGELLEG FSLTKVAGLN ASSKITIFNT SAVENGAFSD LAYPTTKPVT
260 270 280 290 300
FYTYEISDAF KEVILSVQSG VEPKEYPFPA NKFIKGNYYR IKGLKSSTEI
310
EWVLENVEDK EVTLDPFE
Length:318
Mass (Da):35,129
Last modified:July 24, 2007 - v1
Checksum:i0E737FCD8BB2F588
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000140 Genomic DNA. Translation: ABR45223.1.
RefSeqiWP_009275397.1. NC_009615.1.

Genome annotation databases

EnsemblBacteriaiABR45223; ABR45223; BDI_3522.
GeneIDi5308671.
KEGGipdi:BDI_3522.
PATRICi22850268. VBIParDis29947_3487.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000140 Genomic DNA. Translation: ABR45223.1.
RefSeqiWP_009275397.1. NC_009615.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R4RX-ray2.38A/B24-318[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi435591.BDI_3522.

Protocols and materials databases

DNASUi5308671.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR45223; ABR45223; BDI_3522.
GeneIDi5308671.
KEGGipdi:BDI_3522.
PATRICi22850268. VBIParDis29947_3487.

Phylogenomic databases

OrthoDBiPOG091H15ZL.

Enzyme and pathway databases

BioCyciPDIS435591:GCNH-3516-MONOMER.

Miscellaneous databases

EvolutionaryTraceiA6LHQ9.

Family and domain databases

InterProiIPR029141. FimA_N.
[Graphical view]
PfamiPF06321. P_gingi_FimA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFIM1F_PARD8
AccessioniPrimary (citable) accession number: A6LHQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 6, 2016
Last sequence update: July 24, 2007
Last modified: September 7, 2016
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

A propeptide cleavage site can be predicted based on structural similarity with other family members. Still, this protein lacks the lipidation signal found in other family members, suggesting it may not be exported to the cell surface, and may not be part of the fimbriae.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.