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F17a-G fimbrial adhesin

 F17AG_ECOLX             Reviewed;         344 AA.
Q99003; O30927;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 2.
25-OCT-2017, entry version 77.
RecName: Full=F17a-G fimbrial adhesin;
Flags: Precursor;
Name=f17aG;
Escherichia coli.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SIGNAL SEQUENCE CLEAVAGE
SITE, AND SUBCELLULAR LOCATION.
STRAIN=25KH09st/ ETEC;
PubMed=1675211; DOI=10.1128/jb.173.11.3366-3373.1991;
Lintermans P.F.L., Bertels A., Schlicker C., Deboeck F., Charlier G.,
Pohl P., Norgren M., Normark S., van Montagu M., De Greve H.M.J.;
"Identification, characterization, and nucleotide sequence of the F17-
G gene, which determines receptor binding of Escherichia coli F17
fimbriae.";
J. Bacteriol. 173:3366-3373(1991).
[2]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 23-199 AND IN COMPLEX WITH
N-ACETYL-D-GLUCOSAMINE.
STRAIN=25KH09st/ ETEC;
PubMed=12864853; DOI=10.1046/j.1365-2958.2003.03600.x;
Buts L., Bouckaert J., De Genst E., Loris R., Oscarson S., Lahmann M.,
Messens J., Brosens E., Wyns L., De Greve H.M.J.;
"The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an
immunoglobulin-like lectin domain that binds N-acetylglucosamine.";
Mol. Microbiol. 49:705-715(2003).
-!- FUNCTION: Essential fimbrial adhesion factor that mediates binding
to N-acetylglucosamine-containing receptors in the host intestinal
microvilli, leading to colonization of the intestinal tissue, and
diarrhea or septicemia. Also confers adhesiveness to laminin and
basement membranes. {ECO:0000269|PubMed:1675211}.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:1675211}.
Note=Attached to the tip of the fimbrial filaments.
-!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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EMBL; AF022140; AAC45722.1; -; Genomic_DNA.
PIR; A42359; A42359.
RefSeq; WP_061363424.1; NZ_NHTF01000003.1.
PDB; 1O9V; X-ray; 1.75 A; A=23-199.
PDB; 1O9W; X-ray; 1.65 A; A=23-199.
PDB; 1O9Z; X-ray; 1.75 A; A=23-199.
PDB; 1ZPL; X-ray; 1.70 A; A/B=23-199.
PDB; 2BSC; X-ray; 1.40 A; A=23-199.
PDB; 3F64; X-ray; 1.95 A; A=23-199.
PDB; 3F6J; X-ray; 1.75 A; A=23-199.
PDBsum; 1O9V; -.
PDBsum; 1O9W; -.
PDBsum; 1O9Z; -.
PDBsum; 1ZPL; -.
PDBsum; 2BSC; -.
PDBsum; 3F64; -.
PDBsum; 3F6J; -.
ProteinModelPortal; Q99003; -.
SMR; Q99003; -.
PATRIC; fig|562.10497.peg.1043; -.
EvolutionaryTrace; Q99003; -.
GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0044406; P:adhesion of symbiont to host; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 2.60.40.1090; -; 1.
InterPro; IPR008966; Adhesion_dom.
InterPro; IPR000259; Adhesion_dom_fimbrial.
InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
InterPro; IPR015303; Fimbrial_adhesin_lectin_dom.
Pfam; PF09222; Fim-adh_lectin; 1.
Pfam; PF00419; Fimbrial; 1.
SUPFAM; SSF49401; SSF49401; 2.
1: Evidence at protein level;
3D-structure; Disulfide bond; Fimbrium; Lectin; Signal; Virulence.
SIGNAL 1 22 {ECO:0000269|PubMed:1675211}.
CHAIN 23 344 F17a-G fimbrial adhesin.
/FTId=PRO_5000053432.
REGION 23 199 Receptor-binding lectin domain.
REGION 65 66 Carbohydrate binding.
REGION 110 111 Carbohydrate binding.
REGION 139 142 Carbohydrate binding.
REGION 200 344 Fimbrillin-binding domain.
DISULFID 75 132
STRAND 24 26 {ECO:0000244|PDB:2BSC}.
STRAND 30 35 {ECO:0000244|PDB:2BSC}.
STRAND 39 41 {ECO:0000244|PDB:2BSC}.
STRAND 51 53 {ECO:0000244|PDB:1ZPL}.
STRAND 59 71 {ECO:0000244|PDB:2BSC}.
STRAND 75 82 {ECO:0000244|PDB:2BSC}.
STRAND 86 90 {ECO:0000244|PDB:2BSC}.
STRAND 93 112 {ECO:0000244|PDB:2BSC}.
HELIX 113 115 {ECO:0000244|PDB:2BSC}.
STRAND 116 118 {ECO:0000244|PDB:1ZPL}.
STRAND 121 123 {ECO:0000244|PDB:2BSC}.
STRAND 125 132 {ECO:0000244|PDB:2BSC}.
STRAND 138 153 {ECO:0000244|PDB:2BSC}.
STRAND 160 162 {ECO:0000244|PDB:2BSC}.
STRAND 165 174 {ECO:0000244|PDB:2BSC}.
STRAND 186 191 {ECO:0000244|PDB:2BSC}.
STRAND 194 196 {ECO:0000244|PDB:2BSC}.
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


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