ID   PAPG3_ECOLX             Reviewed;         335 AA.
AC   P42188;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Fimbrial adhesin PapGIII {ECO:0000303|PubMed:31361021};
DE   AltName: Full=Adhesin;
DE   Flags: Precursor;
GN   Name=papGIII {ECO:0000303|PubMed:31361021};
GN   Synonyms=prsG {ECO:0000303|PubMed:7902954};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1442;
RX   PubMed=1357526; DOI=10.1111/j.1365-2958.1992.tb01399.x;
RA   Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M., Lindberg F.,
RA   Gaastra W., Normark S.;
RT   "Horizontal gene transfer of the Escherichia coli pap and prs pili operons
RT   as a mechanism for the development of tissue-specific adhesive
RT   properties.";
RL   Mol. Microbiol. 6:2225-2242(1992).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 700336 / J96 / UPEC;
RX   PubMed=1693334; DOI=10.1002/j.1460-2075.1990.tb08328.x;
RA   Stroemberg N., Marklund B.I., Lund B., Ilver D., Hamers A., Gaastra W.,
RA   Karlsson K.A., Normark S.;
RT   "Host-specificity of uropathogenic Escherichia coli depends on differences
RT   in binding specificity to Gal alpha 1-4Gal-containing isoreceptors.";
RL   EMBO J. 9:2001-2010(1990).
RN   [3]
RP   FUNCTION.
RX   PubMed=7902954; DOI=10.1006/mpat.1993.1062;
RA   Johanson I.M., Plos K., Marklund B.I., Svanborg C.;
RT   "Pap, papG and prsG DNA sequences in Escherichia coli from the fecal flora
RT   and the urinary tract.";
RL   Microb. Pathog. 15:121-129(1993).
RN   [4]
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).
CC   -!- FUNCTION: Tip adhesin component of type P pili that binds
CC       preferentially to Gal-alpha(1-4)-Gal-containing glycolipids such as
CC       globoside (PubMed:1693334, PubMed:31361021). This tip is common in
CC       E.coli strains that cause human cystitis, but rare in pyelonephritic
CC       isolates (PubMed:7902954). {ECO:0000269|PubMed:1693334,
CC       ECO:0000269|PubMed:31361021, ECO:0000269|PubMed:7902954}.
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   -!- SIMILARITY: Belongs to the adhesin PapG family. {ECO:0000305}.
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DR   EMBL; X62158; CAA44089.1; -; Genomic_DNA.
DR   PIR; S25212; S25212.
DR   AlphaFoldDB; P42188; -.
DR   SMR; P42188; -.
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:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell adhesion; Fimbrium; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..335
FT                   /note="Fimbrial adhesin PapGIII"
FT                   /id="PRO_0000022155"
SQ   SEQUENCE   335 AA;  37170 MW;  B473E1C87705C11E CRC64;
     MKKWLPAFLF LSLSGCNDAL AANQSTMFYS FNDNIYRPQL SVKVTDIVQF IVDINSASST
     ATLSYVACNG FTWTHGLYWS EYFAWLVVPK HVSYNGYNIY LELQSRGSFS LDAEDNDNYY
     LTKGFAWDEA NTSGQTCFNI GEKRSLAWSF GGVTLNARLP VDLPKGDYTF PVKFLRGIQR
     NNYDYIGGRY KIPSSLMKTF PFNGTLNFSI KNTGGCRPSA QSLEINHGDL SINSANNHYA
     AQTLSVSCDV PTNIRFFLLS NTNPAYSHGQ QFSVGLGHGW DSIISINGVD TGETTMRWYR
     AGTQNLTTGS RLYGESSKIQ PGVLSGSATL LMILP