ID   AFAE1_ECOLX             Reviewed;         161 AA.
AC   P08180; Q47034;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Afimbrial adhesin AFA-I;
DE   AltName: Full=Dr hemagglutinin AFA-I;
DE   Flags: Precursor;
GN   Name=afaE1; Synonyms=afaE, afaE-1;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152.
RC   STRAIN=KS52;
RX   PubMed=2860096; DOI=10.1128/jb.162.3.1285-1292.1985;
RA   Labigne-Roussel A., Schmidt M.A., Walz W., Falkow S.;
RT   "Genetic organization of the afimbrial adhesin operon and nucleotide
RT   sequence from a uropathogenic Escherichia coli gene encoding an afimbrial
RT   adhesin.";
RL   J. Bacteriol. 162:1285-1292(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KS52;
RX   PubMed=7901162; DOI=10.1128/iai.61.12.5106-5114.1993;
RA   le Bouguenec C.L., Garcia M.-I., Ouin V., Desperrier J.-M., Gounon P.,
RA   Labigne A.;
RT   "Characterization of plasmid-borne afa-3 gene clusters encoding afimbrial
RT   adhesins expressed by Escherichia coli strains associated with intestinal
RT   or urinary tract infections.";
RL   Infect. Immun. 61:5106-5114(1993).
CC   -!- FUNCTION: Hemagglutinins of uropathogenic E.coli mediate adherence to
CC       the upper urinary tract. These adhesins bind to the Dr blood group
CC       antigen and also agglutinate human erythrocytes in the presence of D-
CC       mannose (mannose-resistant hemagglutination (MRHA)).
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the Dr-adhesin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA23981.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M12868; AAA23981.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X69197; CAA48941.1; -; Genomic_DNA.
DR   PIR; S42624; HMECA1.
DR   RefSeq; WP_000731739.1; NZ_WNUB01000053.1.
DR   AlphaFoldDB; P08180; -.
DR   SMR; P08180; -.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.60.40.1570; -; 1.
DR   InterPro; IPR006713; Adhesin_Dr.
DR   InterPro; IPR021020; Adhesin_Dr_signal_peptide.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR037028; Dr_adhesin_sf.
DR   Pfam; PF04619; Adhesin_Dr; 1.
DR   Pfam; PF12393; Dr_adhesin; 1.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   3: Inferred from homology;
KW   Fimbrium; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..161
FT                   /note="Afimbrial adhesin AFA-I"
FT                   /id="PRO_0000000872"
SQ   SEQUENCE   161 AA;  17184 MW;  9324B7BE7C7D47B6 CRC64;
     MKKLAIIGAT SVMMMTGTAQ ANFTSSGTNG KVDLTITEEC RVTVESKSES FLRSGLVANR
     HITNLGIQST GCGTGQRVAL KLGAGSYDDT NGAHMTHENG TDKLLVSMGS ATGDGTQDGG
     VYYINRDGNW NGQMVFIVRN DQQHLPTGKY TLNLEGGFWT K