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Protein

F17b-G fimbrial adhesin

Gene

f17bG

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Essential fimbrial adhesion factor that mediates binding to N-acetylglucosamine-containing receptors in the host intestinal microvilli, leading to colonization of the intestinal tissue, and diarrhea or septicemia. Also confers adhesiveness to laminin and basement membranes.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
F17b-G fimbrial adhesin
Gene namesi
Name:f17bG
Encoded oniPlasmid Vir0 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Fimbrium By similarity

  • Note: Attached to the tip of the fimbrial filaments.By similarity

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 – 2222By similarityAdd
BLAST
Chaini23 – 343321F17b-G fimbrial adhesinPRO_5000142177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 132

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 263Combined sources
Beta strandi30 – 356Combined sources
Beta strandi39 – 435Combined sources
Beta strandi49 – 535Combined sources
Beta strandi59 – 7315Combined sources
Beta strandi75 – 828Combined sources
Beta strandi86 – 905Combined sources
Beta strandi93 – 11220Combined sources
Helixi113 – 1153Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi135 – 15016Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi164 – 17310Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi193 – 1975Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BS7X-ray2.10123-198[»]
2BS8X-ray2.25A23-198[»]
3FFOX-ray2.10A23-198[»]
4K0OX-ray2.15A23-198[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47200.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 199177Receptor-binding lectin domainAdd
BLAST
Regioni65 – 662Carbohydrate binding
Regioni110 – 1112Carbohydrate binding
Regioni138 – 1414Carbohydrate binding
Regioni200 – 343144Fimbrillin-binding domainAdd
BLAST

Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
2.60.40.1410. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
IPR015303. Fimbrial_adhesin_lectin_dom.
[Graphical view]
PfamiPF09222. Fim-adh_lectin. 1 hit.
PF00419. Fimbrial. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q47200-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNFYKVFLA VFILVCCNIS HAVVSFIGST ENDVGPSQGS YSSTHAMDNL
60 70 80 90 100
PFVYNTGYNI GYQNANVWRI GGGFCVGLDG KVDLPVVGSL DGQSIYGLTE
110 120 130 140 150
EVGLLIWMGD TNYSRGTAMS GNSWENVFSG WCVGNYLSTQ GLSVHVRPVI
160 170 180 190 200
LKRNSSAQYS VQKTSIGSIR MRPYNGSSAG SVQTTVNFSL NPFTLNDTVT
210 220 230 240 250
SCRLLTPSAV NVSLAAISAG QLPSSGDEVV AGTTSLKLQC DAGVTVWATL
260 270 280 290 300
TDATTPSNRS DILTLTGAST ATGVGLRIYK NTDSTPLKFG PDSPVKGNEN
310 320 330 340
QWQLSTGTET SPSVRLYVKY VNTGEGINPG TVNGISTFTF SYQ
Length:343
Mass (Da):36,418
Last modified:December 16, 2008 - v2
Checksum:i7ECB996497B3F71A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14319 Genomic DNA. Translation: AAA23736.1.
PIRiI41205.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14319 Genomic DNA. Translation: AAA23736.1.
PIRiI41205.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BS7X-ray2.10123-198[»]
2BS8X-ray2.25A23-198[»]
3FFOX-ray2.10A23-198[»]
4K0OX-ray2.15A23-198[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ47200.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
2.60.40.1410. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
IPR015303. Fimbrial_adhesin_lectin_dom.
[Graphical view]
PfamiPF09222. Fim-adh_lectin. 1 hit.
PF00419. Fimbrial. 1 hit.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "F17-like fimbriae from an invasive Escherichia coli strain producing cytotoxic necrotizing factor type 2 toxin."
    el Mazouari K., Oswald E., Hernalsteens J.-P., Lintermans P.F.L., De Greve H.M.J.
    Infect. Immun. 62:2633-2638(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: S5 / EIEC.
  2. "Impact of natural variation in bacterial F17G adhesins on crystallization behaviour."
    Buts L., Wellens A., Van Molle I., Wyns L., Loris R., Lahmann M., Oscarson S., De Greve H.M.J., Bouckaert J.
    Acta Crystallogr. D 61:1149-1159(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 23-198 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.

Entry informationi

Entry nameiF17BG_ECOLX
AccessioniPrimary (citable) accession number: Q47200
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: January 7, 2015
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

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.