Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

F17a-G fimbrial adhesin

Gene

f17aG

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:
F17a-G fimbrial adhesin
Gene namesi
Name:f17aG
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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 – 22221 PublicationAdd
BLAST
Chaini23 – 344322F17a-G fimbrial adhesinPRO_5000053432Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 263Combined sources
Beta strandi30 – 356Combined sources
Beta strandi39 – 413Combined sources
Beta strandi51 – 533Combined sources
Beta strandi59 – 7113Combined 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 strandi138 – 15316Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi165 – 17410Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O9VX-ray1.75A23-199[»]
1O9WX-ray1.65A23-199[»]
1O9ZX-ray1.75A23-199[»]
1ZPLX-ray1.70A/B23-199[»]
2BSCX-ray1.40A23-199[»]
3F64X-ray1.95A23-199[»]
3F6JX-ray1.75A23-199[»]
ProteinModelPortaliQ99003.
SMRiQ99003. Positions 23-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99003.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 199177Receptor-binding lectin domainAdd
BLAST
Regioni65 – 662Carbohydrate binding
Regioni110 – 1112Carbohydrate binding
Regioni139 – 1424Carbohydrate binding
Regioni200 – 344145Fimbrillin-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.

Q99003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNFYKVFLA VFILVCCNIS QAAVSFIGST ENDVGPSLGS YSRTHAMDNL
60 70 80 90 100
PFVYDTRNKI GYQNANVWHI SKGFCVGLDG KVDLPVVGSL DGQSIYGLTE
110 120 130 140 150
EVGLLIWMGD TKYSRGTAMS GNSWENVFSG WCVGANTAST QGLSVRVTPV
160 170 180 190 200
ILKRNSSARY SVQKTSIGSI RMRPYNGSSA GSVQTTVNFS LNPFTLNDTV
210 220 230 240 250
TSCRLLTPSA VNVSLAAISA GQLPSSGDEV VAGTTSLKLQ CDAGVTVWAT
260 270 280 290 300
LTDATTPSNR SDILTLTGAS TATGVGLRIY KNTDSTPLKF GPDSPVKGNE
310 320 330 340
NQWQLSTGTE TSPSVRLYVK YVNTGEGINP GTVNGISTFT FSYQ
Length:344
Mass (Da):36,555
Last modified:August 1, 1998 - v2
Checksum:i632952BEBD0F32FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022140 Genomic DNA. Translation: AAC45722.1.
PIRiA42359.
RefSeqiWP_061363424.1. NZ_LOOH01000015.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022140 Genomic DNA. Translation: AAC45722.1.
PIRiA42359.
RefSeqiWP_061363424.1. NZ_LOOH01000015.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O9VX-ray1.75A23-199[»]
1O9WX-ray1.65A23-199[»]
1O9ZX-ray1.75A23-199[»]
1ZPLX-ray1.70A/B23-199[»]
2BSCX-ray1.40A23-199[»]
3F64X-ray1.95A23-199[»]
3F6JX-ray1.75A23-199[»]
ProteinModelPortaliQ99003.
SMRiQ99003. Positions 23-198.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ99003.

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...

Entry informationi

Entry nameiF17AG_ECOLX
AccessioniPrimary (citable) accession number: Q99003
Secondary accession number(s): O30927
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 71 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

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.