ID   F17BG_ECOLX             Reviewed;         343 AA.
AC   Q47200;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=F17b-G fimbrial adhesin;
DE   Flags: Precursor;
GN   Name=f17bG;
OS   Escherichia coli.
OG   Plasmid Vir.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=S5 / EIEC;
RX   PubMed=7910597; DOI=10.1128/iai.62.6.2633-2638.1994;
RA   el Mazouari K., Oswald E., Hernalsteens J.-P., Lintermans P.F.L.,
RA   De Greve H.M.J.;
RT   "F17-like fimbriae from an invasive Escherichia coli strain producing
RT   cytotoxic necrotizing factor type 2 toxin.";
RL   Infect. Immun. 62:2633-2638(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.25 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. {ECO:0000269|PubMed:7910597}.
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; L14319; AAA23736.1; -; Genomic_DNA.
DR   PIR; I41205; I41205.
DR   PDB; 2BS7; X-ray; 2.10 A; 1=23-198.
DR   PDB; 2BS8; X-ray; 2.25 A; A=23-198.
DR   PDB; 3FFO; X-ray; 2.10 A; A=23-198.
DR   PDB; 4K0O; X-ray; 2.15 A; A=23-198.
DR   PDBsum; 2BS7; -.
DR   PDBsum; 2BS8; -.
DR   PDBsum; 3FFO; -.
DR   PDBsum; 4K0O; -.
DR   AlphaFoldDB; Q47200; -.
DR   SMR; Q47200; -.
DR   UniLectin; Q47200; -.
DR   EvolutionaryTrace; Q47200; -.
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; Plasmid; Signal; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..343
FT                   /note="F17b-G fimbrial adhesin"
FT                   /id="PRO_5000142177"
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:2BS7"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          59..73
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          93..112
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:4K0O"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          125..132
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          135..150
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:2BS8"
FT   STRAND          158..161
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          164..173
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          185..190
FT                   /evidence="ECO:0007829|PDB:2BS7"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:2BS7"
SQ   SEQUENCE   343 AA;  36418 MW;  7ECB996497B3F71A CRC64;
     MTNFYKVFLA VFILVCCNIS HAVVSFIGST ENDVGPSQGS YSSTHAMDNL PFVYNTGYNI
     GYQNANVWRI GGGFCVGLDG KVDLPVVGSL DGQSIYGLTE EVGLLIWMGD TNYSRGTAMS
     GNSWENVFSG WCVGNYLSTQ GLSVHVRPVI LKRNSSAQYS VQKTSIGSIR MRPYNGSSAG
     SVQTTVNFSL NPFTLNDTVT SCRLLTPSAV NVSLAAISAG QLPSSGDEVV AGTTSLKLQC
     DAGVTVWATL TDATTPSNRS DILTLTGAST ATGVGLRIYK NTDSTPLKFG PDSPVKGNEN
     QWQLSTGTET SPSVRLYVKY VNTGEGINPG TVNGISTFTF SYQ