ID   DAAE_ECOLX              Reviewed;         159 AA.
AC   P13719;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=F1845 fimbrial protein;
DE   AltName: Full=Fimbrial adhesin F1845 antigen;
DE   Flags: Precursor;
GN   Name=daaE;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O75:NM / C1845 / DAEC;
RX   PubMed=2568985; DOI=10.1128/jb.171.8.4281-4289.1989;
RA   Bilge S.S., Clausen C.R., Lau W., Moseley S.L.;
RT   "Molecular characterization of a fimbrial adhesin, F1845, mediating diffuse
RT   adherence of diarrhea-associated Escherichia coli to HEp-2 cells.";
RL   J. Bacteriol. 171:4281-4289(1989).
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)). C1845 is a strain
CC       responsible for diarrheal disease.
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the Dr-adhesin family. {ECO:0000305}.
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DR   EMBL; M27725; AAA23661.1; -; Genomic_DNA.
DR   PIR; A33859; A33859.
DR   RefSeq; WP_063611431.1; NZ_LSET01000004.1.
DR   PDB; 2BCM; X-ray; 1.48 A; A/B/C=22-159.
DR   PDBsum; 2BCM; -.
DR   AlphaFoldDB; P13719; -.
DR   SMR; P13719; -.
DR   PRIDE; P13719; -.
DR   EvolutionaryTrace; P13719; -.
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; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..159
FT                   /note="F1845 fimbrial protein"
FT                   /id="PRO_0000000871"
FT   STRAND          23..37
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          61..71
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          100..107
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          128..136
FT                   /evidence="ECO:0007829|PDB:2BCM"
FT   STRAND          145..157
FT                   /evidence="ECO:0007829|PDB:2BCM"
SQ   SEQUENCE   159 AA;  16722 MW;  ABC240A2DB65C2ED CRC64;
     MKKLAIMAAA SMIFTVGSAQ ATFQASGTTG ITTLTVTEEC RVQVGNVTAT LARSKLKDDT
     AIGVIGVTAL GCNGLQAALQ ADPDNYDATN LYMTSRNHDK LNVKLKATDG SSWTYGNGVF
     YKTEGGNWGG HVGISVDGNQ TDKPTGEYTL NLTGGYWTN