F17DG_ECOLX
ID F17DG_ECOLX Reviewed; 344 AA.
AC Q47199;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=F17d-G fimbrial adhesin;
DE Flags: Precursor;
GN Name=f17dG;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=111KH86 / ETEC;
RA De Greve H.M.J., Heng P., Deboeck F., Yan H., Lintermans P.F.L.,
RA Hernalsteens J.-P.;
RT "Molecular and genetic analysis of a F17-related gene cluster.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CRYSTALLIZATION OF 23-198.
RX PubMed=16041081; DOI=10.1107/s0907444905017038;
RA Buts L., Wellens A., Van Molle I., Wyns L., Loris R., Lahmann M.,
RA Oscarson S., De Greve H.M.J., Bouckaert J.;
RT "Impact of natural variation in bacterial F17G adhesins on crystallization
RT behaviour.";
RL Acta Crystallogr. D 61:1149-1159(2005).
CC -!- FUNCTION: Essential fimbrial adhesion factor that mediates binding to
CC N-acetylglucosamine-containing receptors in the host intestinal
CC microvilli, leading to colonization of the intestinal tissue, and
CC diarrhea or septicemia. Also confers adhesiveness to laminin and
CC basement membranes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250}. Note=Attached to the tip
CC of the fimbrial filaments. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR EMBL; L77091; AAA92621.1; -; Genomic_DNA.
DR RefSeq; WP_000181225.1; NZ_WSHD01000026.1.
DR AlphaFoldDB; Q47199; -.
DR SMR; Q47199; -.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0044406; P:adhesion of symbiont to host; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.1090; -; 1.
DR InterPro; IPR000259; Adhesion_dom_fimbrial.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR015303; Fimbrial_adhesin_lectin_dom.
DR Pfam; PF09222; Fim-adh_lectin; 1.
DR Pfam; PF00419; Fimbrial; 1.
DR SUPFAM; SSF49401; SSF49401; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Fimbrium; Lectin; Signal; Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..344
FT /note="F17d-G fimbrial adhesin"
FT /id="PRO_0000356268"
FT REGION 23..199
FT /note="Receptor-binding lectin domain"
FT /evidence="ECO:0000250"
FT REGION 200..344
FT /note="Fimbrillin-binding domain"
FT /evidence="ECO:0000250"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65..66
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 110..111
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 139..142
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT DISULFID 75..132
FT /evidence="ECO:0000250"
SQ SEQUENCE 344 AA; 36430 MW; E8141B488D7A56D6 CRC64;
MTNFYKVFLA VFILVCCNIS QAAVSFIGST ENDVGPSPGS YSRTHAMDNL PFVYNTGNNI
GYQNANVWRI SKGFCVGLDG KVDLPVVGSL DGQSIYGLTE EVGLLIWMGD TNYSRGTAMS
GNSWENVFSG WCVGANTAST QGLSVRVTPV ILKRNSSARY SVQKTSIGSI RMRPYNGSSA
GSVQTTVNFS LNPFTLNDTV TSCRLLTPSA VNVSLAAISA GQLPSSGDEV VAGTTSLKLQ
CDAGVTVWAT LTDATTPSNR SDILTLTGAS TATGVGLRIY KNTDSTPLKF GPDSPVKGNE
NQWQLSTGTE TSPSVRLYVK YVNTGEGINP GTVNGISTFT FSYQ
