ID   F17FG_ECOLX             Reviewed;         343 AA.
AC   Q9RH91;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=F17f-G fimbrial adhesin;
DE   Flags: Precursor;
GN   Name=f17fG;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CK377;
RX   PubMed=10203489; DOI=10.1128/jcm.37.5.1370-1375.1999;
RA   Cid D., Sanz R., Marin I., de Greve H.M.J., Ruiz-Santa-Quiteria J.A.,
RA   Amils R., de la Fuente R.;
RT   "Characterization of nonenterotoxigenic Escherichia coli strains producing
RT   F17 fimbriae isolated from diarrheic lambs and goat kids.";
RL   J. Clin. Microbiol. 37:1370-1375(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 23-198 IN COMPLEX WITH
RP   N-ACETYL-D-GLUCOSAMINE.
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; AF055312; AAD17515.1; -; Genomic_DNA.
DR   PDB; 1ZK5; X-ray; 1.40 A; A=23-198.
DR   PDBsum; 1ZK5; -.
DR   AlphaFoldDB; Q9RH91; -.
DR   SMR; Q9RH91; -.
DR   UniLectin; Q9RH91; -.
DR   EvolutionaryTrace; Q9RH91; -.
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   3D-structure; Disulfide bond; Fimbrium; Lectin; Signal; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..343
FT                   /note="F17f-G fimbrial adhesin"
FT                   /id="PRO_0000356270"
FT   REGION          23..199
FT                   /note="Receptor-binding lectin domain"
FT   REGION          200..343
FT                   /note="Fimbrillin-binding domain"
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   BINDING         110..111
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT   BINDING         138..141
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT   DISULFID        75..132
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          59..71
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          93..112
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          125..132
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          135..152
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          164..174
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          185..190
FT                   /evidence="ECO:0007829|PDB:1ZK5"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:1ZK5"
SQ   SEQUENCE   343 AA;  36380 MW;  19BF1087C03D2A56 CRC64;
     MTNFYKVFLA VFILVCCNIS HAAVSFIGST ENDVGPSQGS YSSTHAMDNL PFVYNTGHNI
     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