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F17b-G fimbrial adhesin

 F17BG_ECOLX             Reviewed;         343 AA.
Q47200;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
25-OCT-2017, entry version 69.
RecName: Full=F17b-G fimbrial adhesin;
Flags: Precursor;
Name=f17bG;
Escherichia coli.
Plasmid Vir.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=S5 / EIEC;
PubMed=7910597;
el Mazouari K., Oswald E., Hernalsteens J.-P., Lintermans P.F.L.,
De Greve H.M.J.;
"F17-like fimbriae from an invasive Escherichia coli strain producing
cytotoxic necrotizing factor type 2 toxin.";
Infect. Immun. 62:2633-2638(1994).
[2]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 23-198 IN COMPLEX WITH
N-ACETYL-D-GLUCOSAMINE.
PubMed=16041081; DOI=10.1107/S0907444905017038;
Buts L., Wellens A., Van Molle I., Wyns L., Loris R., Lahmann M.,
Oscarson S., De Greve H.M.J., Bouckaert J.;
"Impact of natural variation in bacterial F17G adhesins on
crystallization behaviour.";
Acta Crystallogr. D 61:1149-1159(2005).
-!- 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:7910597}.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250}. Note=Attached to the
tip of the fimbrial filaments. {ECO:0000250}.
-!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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EMBL; L14319; AAA23736.1; -; Genomic_DNA.
PIR; I41205; I41205.
PDB; 2BS7; X-ray; 2.10 A; 1=23-198.
PDB; 2BS8; X-ray; 2.25 A; A=23-198.
PDB; 3FFO; X-ray; 2.10 A; A=23-198.
PDB; 4K0O; X-ray; 2.15 A; A=23-198.
PDBsum; 2BS7; -.
PDBsum; 2BS8; -.
PDBsum; 3FFO; -.
PDBsum; 4K0O; -.
SMR; Q47200; -.
EvolutionaryTrace; Q47200; -.
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; Plasmid; Signal;
Virulence.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 343 F17b-G fimbrial adhesin.
/FTId=PRO_5000142177.
REGION 23 199 Receptor-binding lectin domain.
REGION 65 66 Carbohydrate binding.
REGION 110 111 Carbohydrate binding.
REGION 138 141 Carbohydrate binding.
REGION 200 343 Fimbrillin-binding domain.
DISULFID 75 132
STRAND 24 26 {ECO:0000244|PDB:2BS7}.
STRAND 30 35 {ECO:0000244|PDB:2BS7}.
STRAND 39 43 {ECO:0000244|PDB:2BS7}.
STRAND 49 53 {ECO:0000244|PDB:2BS7}.
STRAND 59 73 {ECO:0000244|PDB:2BS7}.
STRAND 75 82 {ECO:0000244|PDB:2BS7}.
STRAND 86 90 {ECO:0000244|PDB:2BS7}.
STRAND 93 112 {ECO:0000244|PDB:2BS7}.
HELIX 113 115 {ECO:0000244|PDB:2BS7}.
STRAND 116 118 {ECO:0000244|PDB:4K0O}.
STRAND 121 123 {ECO:0000244|PDB:2BS7}.
STRAND 125 132 {ECO:0000244|PDB:2BS7}.
STRAND 135 150 {ECO:0000244|PDB:2BS7}.
STRAND 155 157 {ECO:0000244|PDB:2BS8}.
STRAND 158 161 {ECO:0000244|PDB:2BS7}.
STRAND 164 173 {ECO:0000244|PDB:2BS7}.
STRAND 185 190 {ECO:0000244|PDB:2BS7}.
STRAND 193 197 {ECO:0000244|PDB:2BS7}.
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


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