ID   F17CG_ECOLX             Reviewed;         343 AA.
AC   Q47033;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=F17c-G fimbrial adhesin;
DE   AltName: Full=Adhesin 20K;
DE   Flags: Precursor;
GN   Name=f17cG;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ADHESION TO HOST CELLS.
RC   STRAIN=31A/o6;
RX   PubMed=9404505; DOI=10.1016/s0923-2508(97)81900-6;
RA   Martin C., Rousset E., De Greve H.M.J.;
RT   "Human uropathogenic and bovine septicaemic Escherichia coli strains carry
RT   an identical F17-related adhesin.";
RL   Res. Microbiol. 148:55-64(1997).
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       ECO:0000269|PubMed:9404505}.
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; L43374; AAA85086.1; -; Genomic_DNA.
DR   RefSeq; WP_012775842.1; NZ_WTSK01000051.1.
DR   AlphaFoldDB; Q47033; -.
DR   SMR; Q47033; -.
DR   PATRIC; fig|562.7958.peg.4039; -.
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..343
FT                   /note="F17c-G fimbrial adhesin"
FT                   /id="PRO_0000356267"
FT   REGION          23..199
FT                   /note="Receptor-binding lectin domain"
FT                   /evidence="ECO:0000250"
FT   REGION          200..343
FT                   /note="Fimbrillin-binding domain"
FT                   /evidence="ECO:0000250"
FT   REGION          287..307
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         138..141
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..132
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  36406 MW;  72C04F2235397E43 CRC64;
     MTNFYKVFLA VFILVCCNIS HAAVSFIGST ENDVGPSQGS YSSTHAMDNL PFVYNTGYNI
     GYQNANVWRI SGGFCVGLDG KVDLPVVGSL DGQSIYGLTE EVGLLIWMGD TNYSRGTAMS
     GNSWENVFSG WCVGNYVSTQ GLSVHVRPVI LKRNSSAQYS VQKTSIGSIR MRPYNGSSAG
     SVQTTVNFSL NPFTLNDTVT SCRLLTPSAV NVSLAAISAG QLPSSGDEVV AGTTSLKLQC
     DAGVTVWATL TDATTPSNRS DILTLTGAST ATGVGLRIYK NTDSTPLKFG PDSPVKGNEN
     QWQLSTGTET SPSVRLYVKY VNTGEGINPG TVNGISTFTF SYQ