ID   SFAA_ECOL5              Reviewed;         181 AA.
AC   P12730; Q0TL53;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=S-fimbrial protein subunit SfaA;
DE   AltName: Full=S-fimbrillin;
DE   Flags: Precursor;
GN   Name=sfaA; OrderedLocusNames=ECP_0293;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Schmoll T., Hacker J., Goebel W.;
RT   "Nucleotide sequence of the sfaA gene coding for the S-fimbrial protein
RT   subunit of Escherichia coli.";
RL   FEMS Microbiol. Lett. 41:229-235(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
RN   [3]
RP   SUBCELLULAR LOCATION, IDENTIFICATION IN FIMBRIAE COMPLEX, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=2576095; DOI=10.1111/j.1365-2958.1989.tb00159.x;
RA   Schmoll T., Hoschuetzky H., Morschhaeuser J., Lottspeich F., Jann K.,
RA   Hacker J.;
RT   "Analysis of genes coding for the sialic acid-binding adhesin and two other
RT   minor fimbrial subunits of the S-fimbrial adhesin determinant of
RT   Escherichia coli.";
RL   Mol. Microbiol. 3:1735-1744(1989).
CC   -!- FUNCTION: Fimbriae (also called pili), polar filaments radiating from
CC       the surface of the bacterium to a length of 0.5-1.5 micrometers and
CC       numbering 100-300 per cell, enable bacteria to colonize the epithelium
CC       of specific host organs.
CC   -!- FUNCTION: The major fimbrial subunit. Interacts with alpha-sialic acid-
CC       (2-3)-beta-Gal containing receptors. It belongs to the group of Mrh
CC       (Mannose-resistant hemagglutination) fimbrial proteins.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:2576095}.
CC   -!- DISRUPTION PHENOTYPE: Deletion leads to loss of fimbriation and a
CC       decrease of hemagglutination. {ECO:0000269|PubMed:2576095}.
CC   -!- MISCELLANEOUS: This protein belongs to the group of SfA (S-fimbrial
CC       adhesins), which are associated with uropathogenic strains and with
CC       strains causing newborn meningitis.
CC   -!- SIMILARITY: Belongs to the fimbrial protein 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; M35273; AAA24626.1; -; Genomic_DNA.
DR   EMBL; X17420; CAA35468.1; -; Genomic_DNA.
DR   EMBL; CP000247; ABG68328.1; -; Genomic_DNA.
DR   PIR; S00352; YQECFA.
DR   RefSeq; WP_000768216.1; NC_008253.1.
DR   AlphaFoldDB; P12730; -.
DR   SMR; P12730; -.
DR   STRING; 362663.ECP_0293; -.
DR   EnsemblBacteria; ABG68328; ABG68328; ECP_0293.
DR   KEGG; ecp:ECP_0293; -.
DR   HOGENOM; CLU_088965_0_0_6; -.
DR   OMA; DAACAVN; -.
DR   Proteomes; UP000009182; Chromosome.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.1090; -; 1.
DR   InterPro; IPR000259; Adhesion_dom_fimbrial.
DR   InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   Pfam; PF00419; Fimbrial; 1.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Fimbrium; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..181
FT                   /note="S-fimbrial protein subunit SfaA"
FT                   /id="PRO_0000009200"
FT   DISULFID        44..84
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55..57
FT                   /note="VLL -> FS (in Ref. 1; AAA24626/CAA35468)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   181 AA;  18491 MW;  29442E9EE9BFB9CB CRC64;
     MKLKFISMAV FSALTLGVAT NASAVTTVNG GTVHFKGEVV DAACAVNTNS ANQTVLLGQV
     RSAKLANDGE KSSPVGFSIE LNDCSSATAG HASIIFAGNV IATHNDVLSL QNSAAGSATN
     VGIQILDHTG TAVQFDGVTA STQFTLTDGT NKIPFQAVYY ATGKSTPGIA NADATFKVQY
     Q