ID   AFAE3_ECOLX             Reviewed;         160 AA.
AC   Q57254;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Afimbrial adhesin AFA-III;
DE   Flags: Precursor;
GN   Name=afaE3; Synonyms=afaE-3;
OS   Escherichia coli.
OG   Plasmid pIL1055.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A30 / UPEC;
RX   PubMed=8002584; DOI=10.1128/jb.176.24.7601-7613.1994;
RA   Garcia M.-I., Labigne A., le Bouguenec C.L.;
RT   "Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster
RT   and its translocation via flanking IS1 insertion sequences.";
RL   J. Bacteriol. 176:7601-7613(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=A30 / UPEC, AL845, and AL847;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X76688; CAA54121.1; -; Genomic_DNA.
DR   EMBL; X69102; CAA48847.1; -; Genomic_DNA.
DR   PIR; H55545; H55545.
DR   PDB; 1RXL; NMR; -; A=38-160.
DR   PDB; 1USZ; X-ray; 3.28 A; A=21-160.
DR   PDB; 1UT2; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I=21-160.
DR   PDB; 2IXQ; NMR; -; B=38-160.
DR   PDB; 2VER; NMR; -; A=38-160.
DR   PDBsum; 1RXL; -.
DR   PDBsum; 1USZ; -.
DR   PDBsum; 1UT2; -.
DR   PDBsum; 2IXQ; -.
DR   PDBsum; 2VER; -.
DR   AlphaFoldDB; Q57254; -.
DR   BMRB; Q57254; -.
DR   SMR; Q57254; -.
DR   IntAct; Q57254; 1.
DR   DrugBank; DB08217; S-[(1-Hydroxy-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate.
DR   EvolutionaryTrace; Q57254; -.
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   1: Evidence at protein level;
KW   3D-structure; Fimbrium; Plasmid; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..160
FT                   /note="Afimbrial adhesin AFA-III"
FT                   /id="PRO_0000000873"
FT   REGION          22..75
FT                   /note="Receptor-binding"
FT                   /evidence="ECO:0000250"
FT   VARIANT         59
FT                   /note="A -> T (in strain: AL847)"
FT   VARIANT         73
FT                   /note="N -> D (in strain: AL845 and AL847; chloramphenicol-
FT                   sensitive)"
FT   STRAND          22..37
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:1UT2"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:1UT2"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:1RXL"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          101..111
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          120..125
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:1USZ"
FT   STRAND          146..159
FT                   /evidence="ECO:0007829|PDB:1USZ"
SQ   SEQUENCE   160 AA;  17075 MW;  D5228F367A9D0275 CRC64;
     MKKLAIMAAA SMVFAVSSAH AGFTPSGTTG TTKLTVTEEC QVRVGDLTVA KTRGQLTDAA
     PIGPVTVQAL GCNARQVALK ADTDNFEQGK FFLISDNNRD KLYVNIRPMD NSAWTTDNGV
     FYKNDVGSWG GTIGIYVDGQ QTNTPPGNYT LTLTGGYWAK