PAPG2_ECOLX
ID PAPG2_ECOLX Reviewed; 336 AA.
AC Q47450;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Fimbrial adhesin PapGII {ECO:0000303|PubMed:31361021};
DE Flags: Precursor;
GN Name=papGII {ECO:0000303|PubMed:31361021};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AD110 / UPEC;
RX PubMed=2895103; DOI=10.1128/jb.170.4.1887-1894.1988;
RA Lund B., Lindberg F., Normark S.;
RT "Structure and antigenic properties of the tip-located P pilus proteins of
RT uropathogenic Escherichia coli.";
RL J. Bacteriol. 170:1887-1894(1988).
RN [2]
RP FUNCTION.
RX PubMed=31361021; DOI=10.1093/glycob/cwz059;
RA Legros N., Ptascheck S., Pohlentz G., Karch H., Dobrindt U., Muething J.;
RT "PapG subtype-specific binding characteristics of Escherichia coli towards
RT globo-series glycosphingolipids of human kidney and bladder uroepithelial
RT cells.";
RL Glycobiology 29:789-802(2019).
RN [3] {ECO:0007744|PDB:1J8R, ECO:0007744|PDB:1J8S}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-216 IN COMPLEX WITH GALACTOSE,
RP DISULFIDE BONDS, FUNCTION, AND MUTAGENESIS OF TRP-127 AND ARG-190.
RX PubMed=11440716; DOI=10.1016/s0092-8674(01)00388-9;
RA Dodson K.W., Pinkner J.S., Rose T., Magnusson G., Hultgren S.J.,
RA Waksman G.;
RT "Structural basis of the interaction of the pyelonephritic E. coli adhesin
RT to its human kidney receptor.";
RL Cell 105:733-743(2001).
RN [4] {ECO:0007744|PDB:6CD2}
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 21-336, AND DISULFIDE BONDS.
RX PubMed=30275511; DOI=10.1038/s41564-018-0255-y;
RA Omattage N.S., Deng Z., Pinkner J.S., Dodson K.W., Almqvist F., Yuan P.,
RA Hultgren S.J.;
RT "Structural basis for usher activation and intramolecular subunit transfer
RT in P pilus biogenesis in Escherichia coli.";
RL Nat. Microbiol. 3:1362-1368(2018).
CC -!- FUNCTION: Tip adhesin component of type P pili that plays a critical
CC role in kidney infection through targeted interaction with the
CC globoseries glycolipids containing the Gal-alpha(1-4)-Gal disaccharide
CC present on uroepithelial cells (PubMed:11440716, PubMed:31361021). In
CC turn, transcriptionally regulates host gene expression in kidney cells,
CC leading to inflammatory pathway activation and renal tissue damage.
CC Acts thereby as key determinant of invasive uropathogenic E.coli
CC (UPEC), which cause pyelonephritis and urinary-source bacteremia (By
CC similarity). {ECO:0000250|UniProtKB:A0A0H2VAQ6,
CC ECO:0000269|PubMed:11440716, ECO:0000269|PubMed:31361021}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13720}. Fimbrium
CC {ECO:0000250|UniProtKB:P13720}. Note=At the tip of P pili.
CC {ECO:0000250|UniProtKB:P13720}.
CC -!- MISCELLANEOUS: Strains of E.coli that cause infection of the human
CC urinary tract produce pap-pili (P pili) which are hair-like appendages
CC consisting of about 1000 helically arranged subunits of the protein
CC PapA. These pili mediate binding to digalactoside-containing
CC glycolipids present on the epithelial cells which line the urinary
CC tract.
CC -!- SIMILARITY: Belongs to the adhesin PapG family. {ECO:0000305}.
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DR EMBL; M20182; AAA24296.1; -; Genomic_DNA.
DR PIR; H27743; H27743.
DR PIR; I27743; I27743.
DR PDB; 1J8R; X-ray; 1.80 A; A=21-216.
DR PDB; 1J8S; X-ray; 2.10 A; A=21-216.
DR PDB; 3ME0; X-ray; 2.03 A; B=215-336.
DR PDB; 6CD2; X-ray; 3.70 A; B=21-336.
DR PDB; 7LHG; EM; 3.80 A; G=1-336.
DR PDB; 7LHH; EM; 7.20 A; G=1-336.
DR PDB; 7LHI; EM; 7.60 A; G=1-336.
DR PDBsum; 1J8R; -.
DR PDBsum; 1J8S; -.
DR PDBsum; 3ME0; -.
DR PDBsum; 6CD2; -.
DR PDBsum; 7LHG; -.
DR PDBsum; 7LHH; -.
DR PDBsum; 7LHI; -.
DR AlphaFoldDB; Q47450; -.
DR SMR; Q47450; -.
DR IntAct; Q47450; 1.
DR UniLectin; Q47450; -.
DR EvolutionaryTrace; Q47450; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00239; PapG_CBD; 1.
DR Gene3D; 2.60.40.1090; -; 1.
DR Gene3D; 2.60.40.1370; -; 1.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR005310; PapG_carb-bd_N.
DR InterPro; IPR038420; PapG_carbohydrate-bd_sf.
DR InterPro; IPR005309; PapG_chaper-bd_C.
DR Pfam; PF03628; PapG_C; 1.
DR Pfam; PF03627; PapG_N; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Fimbrium; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..336
FT /note="Fimbrial adhesin PapGII"
FT /evidence="ECO:0000255"
FT /id="PRO_5004233089"
FT BINDING 79
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0007744|PDB:1J8R"
FT BINDING 124..127
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0007744|PDB:1J8R"
FT DISULFID 64..138
FT /evidence="ECO:0000269|PubMed:30275511,
FT ECO:0007744|PDB:1J8R, ECO:0007744|PDB:1J8S,
FT ECO:0007744|PDB:6CD2"
FT DISULFID 217..249
FT /evidence="ECO:0000269|PubMed:30275511,
FT ECO:0007744|PDB:6CD2"
FT MUTAGEN 127
FT /note="W->A: Abolished receptor binding activity."
FT /evidence="ECO:0000269|PubMed:11440716"
FT MUTAGEN 190
FT /note="R->A: Abolished receptor binding activity."
FT /evidence="ECO:0000269|PubMed:11440716"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1J8S"
FT STRAND 76..91
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 116..131
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 166..186
FT /evidence="ECO:0007829|PDB:1J8R"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1J8R"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 292..315
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3ME0"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:3ME0"
SQ SEQUENCE 336 AA; 37667 MW; DF6047C92C3F9BAA CRC64;
MKKWFPALLF SLCVSGESSA WNNIVFYSLG DVNSYQGGNV VITQRPQFIT SWRPGIATVT
WNQCNGPEFA DGFWAYYREY IAWVVFPKKV MTQNGYPLFI EVHNKGSWSE ENTGDNDSYF
FLKGYKWDER AFDAGNLCQK PGEITRLTEK FDDIIFKVAL PADLPLGDYS VKIPYTSGMQ
RHFASYLGAR FKIPYNVAKT LPRENEMLFL FKNIGGCRPS AQSLEIKHGD LSINSANNHY
AAQTLSVSCD VPANIRFMLL RNTTPTYSHG KKFSVGLGHG WDSIVSVNGV DTGETTMRWY
KAGTQNLTIG SRLYGESSKI QPGVLSGSAT LLMILP
