F17AG_ECOLX
ID F17AG_ECOLX Reviewed; 344 AA.
AC Q99003; O30927;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=F17a-G fimbrial adhesin;
DE Flags: Precursor;
GN Name=f17aG;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SIGNAL SEQUENCE CLEAVAGE SITE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=25KH09st/ ETEC;
RX PubMed=1675211; DOI=10.1128/jb.173.11.3366-3373.1991;
RA Lintermans P.F.L., Bertels A., Schlicker C., Deboeck F., Charlier G.,
RA Pohl P., Norgren M., Normark S., van Montagu M., De Greve H.M.J.;
RT "Identification, characterization, and nucleotide sequence of the F17-G
RT gene, which determines receptor binding of Escherichia coli F17 fimbriae.";
RL J. Bacteriol. 173:3366-3373(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 23-199 AND IN COMPLEX WITH
RP N-ACETYL-D-GLUCOSAMINE.
RC STRAIN=25KH09st/ ETEC;
RX PubMed=12864853; DOI=10.1046/j.1365-2958.2003.03600.x;
RA Buts L., Bouckaert J., De Genst E., Loris R., Oscarson S., Lahmann M.,
RA Messens J., Brosens E., Wyns L., De Greve H.M.J.;
RT "The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an
RT immunoglobulin-like lectin domain that binds N-acetylglucosamine.";
RL Mol. Microbiol. 49:705-715(2003).
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:1675211}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:1675211}.
CC Note=Attached to the tip of the fimbrial filaments.
CC -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF022140; AAC45722.1; -; Genomic_DNA.
DR PIR; A42359; A42359.
DR RefSeq; WP_061363424.1; NZ_QLKB01000116.1.
DR PDB; 1O9V; X-ray; 1.75 A; A=23-199.
DR PDB; 1O9W; X-ray; 1.65 A; A=23-199.
DR PDB; 1O9Z; X-ray; 1.75 A; A=23-199.
DR PDB; 1ZPL; X-ray; 1.70 A; A/B=23-199.
DR PDB; 2BSC; X-ray; 1.40 A; A=23-199.
DR PDB; 3F64; X-ray; 1.95 A; A=23-199.
DR PDB; 3F6J; X-ray; 1.75 A; A=23-199.
DR PDBsum; 1O9V; -.
DR PDBsum; 1O9W; -.
DR PDBsum; 1O9Z; -.
DR PDBsum; 1ZPL; -.
DR PDBsum; 2BSC; -.
DR PDBsum; 3F64; -.
DR PDBsum; 3F6J; -.
DR AlphaFoldDB; Q99003; -.
DR SMR; Q99003; -.
DR UniLectin; Q99003; -.
DR PATRIC; fig|562.10497.peg.1043; -.
DR EvolutionaryTrace; Q99003; -.
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:0000269|PubMed:1675211"
FT CHAIN 23..344
FT /note="F17a-G fimbrial adhesin"
FT /id="PRO_5000053432"
FT REGION 23..199
FT /note="Receptor-binding lectin domain"
FT REGION 200..344
FT /note="Fimbrillin-binding domain"
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 BINDING 110..111
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 139..142
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT DISULFID 75..132
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1ZPL"
FT STRAND 59..71
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 93..112
FT /evidence="ECO:0007829|PDB:2BSC"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1ZPL"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 138..153
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2BSC"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2BSC"
SQ SEQUENCE 344 AA; 36555 MW; 632952BEBD0F32FB CRC64;
MTNFYKVFLA VFILVCCNIS QAAVSFIGST ENDVGPSLGS YSRTHAMDNL PFVYDTRNKI
GYQNANVWHI SKGFCVGLDG KVDLPVVGSL DGQSIYGLTE EVGLLIWMGD TKYSRGTAMS
GNSWENVFSG WCVGANTAST QGLSVRVTPV ILKRNSSARY SVQKTSIGSI RMRPYNGSSA
GSVQTTVNFS LNPFTLNDTV TSCRLLTPSA VNVSLAAISA GQLPSSGDEV VAGTTSLKLQ
CDAGVTVWAT LTDATTPSNR SDILTLTGAS TATGVGLRIY KNTDSTPLKF GPDSPVKGNE
NQWQLSTGTE TSPSVRLYVK YVNTGEGINP GTVNGISTFT FSYQ
