ID   SFAS_ECOL5              Reviewed;         163 AA.
AC   P13430; Q0TL48;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=S-fimbrial adhesin protein SfaS;
DE   Flags: Precursor;
GN   Name=sfaS; OrderedLocusNames=ECP_0298;
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], PROTEIN SEQUENCE OF 23-63, SUBCELLULAR
RP   LOCATION, IDENTIFICATION IN FIMBRIAE COMPLEX, AND DISRUPTION 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).
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   MUTAGENESIS OF LYS-138; ARG-140 AND LYS-144.
RX   PubMed=2194961; DOI=10.1128/iai.58.7.2133-2138.1990;
RA   Morschhaeuser J., Hoschuetzky H., Jann K., Hacker J.;
RT   "Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic
RT   Escherichia coli by site-specific mutagenesis.";
RL   Infect. Immun. 58:2133-2138(1990).
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: A minor fimbrial subunit, this protein is necessary for full
CC       expression of S-specific binding. S-fimbrial adhesins enable pathogenic
CC       E.coli causing urinary-tract infections or newborn meningitis to attach
CC       to glycoproteins terminating with alpha-sialic acid-(2-3)-beta-Gal.
CC       This protein binds to the alpha-sialic acid-(2-3)-beta-Gal and is thus
CC       responsible for erythrocyte recognition and hemagglutination.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:2576095}.
CC   -!- DISRUPTION PHENOTYPE: Deletion prevents hemagglutination (erythrocyte
CC       recognition), although cells are still poorly fimbriated.
CC       {ECO:0000269|PubMed:2576095}.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; X16664; CAA34653.1; -; Genomic_DNA.
DR   EMBL; CP000247; ABG68333.1; -; Genomic_DNA.
DR   PIR; S15926; S15926.
DR   RefSeq; WP_000767892.1; NC_008253.1.
DR   AlphaFoldDB; P13430; -.
DR   SMR; P13430; -.
DR   STRING; 362663.ECP_0298; -.
DR   EnsemblBacteria; ABG68333; ABG68333; ECP_0298.
DR   KEGG; ecp:ECP_0298; -.
DR   HOGENOM; CLU_088965_6_1_6; -.
DR   OMA; WITFHIN; -.
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   Direct protein sequencing; Disulfide bond; Fimbrium; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:2576095"
FT   CHAIN           23..163
FT                   /note="S-fimbrial adhesin protein SfaS"
FT                   /id="PRO_0000009202"
FT   REGION          138..144
FT                   /note="Involved in sialic acid binding"
FT   DISULFID        38..75
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         138
FT                   /note="K->T: No change in S-binding."
FT                   /evidence="ECO:0000269|PubMed:2194961"
FT   MUTAGEN         140
FT                   /note="R->S: No hemagglutination, weak reaction with
FT                   antiadhesin-specific antibody A1."
FT                   /evidence="ECO:0000269|PubMed:2194961"
FT   MUTAGEN         144
FT                   /note="K->T: No hemagglutination, no reaction with
FT                   antiadhesin-specific antibody A1."
FT                   /evidence="ECO:0000269|PubMed:2194961"
SQ   SEQUENCE   163 AA;  17183 MW;  0BF1333BF8B2DE4F CRC64;
     MKLKAIILAT GLINCIAFSA QAVDTTITVT GNVLQRTCNV PGNVDVSLGN LYVSDFPNAG
     SGSPWVNFDL SLTGCQNMNT VRATFSGTAD GQTYYANTGN AGGIKIEIQD RDGSNASYHN
     GMFKTLNVQN NNATFNLKAR AVSKGQVTPG NISSVITVTY TYA