F17GG_ECOLX
ID F17GG_ECOLX Reviewed; 343 AA.
AC Q47341;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=F17g-G fimbrial adhesin;
DE AltName: Full=G fimbriae adhesin;
DE AltName: Full=G lectin;
DE Flags: Precursor;
GN Name=f17gG; Synonyms=gafD;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=IH11165 / UPEC;
RX PubMed=7883703; DOI=10.1128/jb.177.6.1477-1484.1995;
RA Saarela S., Taira S., Nurmiaho-Lassila E.L., Makkonen A., Rhen M.;
RT "The Escherichia coli G-fimbrial lectin protein participates both in
RT fimbrial biogenesis and in recognition of the receptor N-acetyl-D-
RT glucosamine.";
RL J. Bacteriol. 177:1477-1484(1995).
RN [2]
RP FUNCTION IN ADHESION TO HOST BASAL MEMBRANE LAMININ.
RX PubMed=8698525; DOI=10.1128/iai.64.7.2857-2860.1996;
RA Saarela S., Westerlund-Wikstroem B., Rhen M., Korhonen T.K.;
RT "The GafD protein of the G (F17) fimbrial complex confers adhesiveness of
RT Escherichia coli to laminin.";
RL Infect. Immun. 64:2857-2860(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 23-200 IN COMPLEX WITH
RP N-ACETYL-D-GLUCOSAMINE, DISULFIDE BOND, AND MUTAGENESIS OF ASP-110.
RX PubMed=12909017; DOI=10.1016/s0022-2836(03)00841-6;
RA Merckel M.C., Tanskanen J., Edelman S., Westerlund-Wikstroem B.,
RA Korhonen T.K., Goldman A.;
RT "The structural basis of receptor-binding by Escherichia coli associated
RT with diarrhea and septicemia.";
RL J. Mol. Biol. 331:897-905(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. May be involved in the initiation of polymerization
CC of fimbrillin monomers during fimbrial filament biogenesis.
CC {ECO:0000269|PubMed:7883703, ECO:0000269|PubMed:8698525}.
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; L33969; AAA69514.1; -; Genomic_DNA.
DR PIR; I55123; I55123.
DR PDB; 1OIO; X-ray; 1.70 A; A/B=23-200.
DR PDBsum; 1OIO; -.
DR AlphaFoldDB; Q47341; -.
DR SMR; Q47341; -.
DR UniLectin; Q47341; -.
DR EvolutionaryTrace; Q47341; -.
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="F17g-G fimbrial adhesin"
FT /id="PRO_0000356271"
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 /evidence="ECO:0000269|PubMed:12909017"
FT MUTAGEN 110
FT /note="D->L: 80% reduction in binding to N-acetyl-D-
FT glucosamine."
FT /evidence="ECO:0000269|PubMed:12909017"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 93..112
FT /evidence="ECO:0007829|PDB:1OIO"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 135..150
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:1OIO"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1OIO"
SQ SEQUENCE 343 AA; 36362 MW; 70E48EE1A18AE8A7 CRC64;
MTNFYKVCLA VFILVCCNIS HAAVSFIGST ENDVGPSQGS YSSTHAMDNL PFVYNTGYNI
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
