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S-fimbrial protein subunit SfaA (S-fimbrillin)

 SFAA_ECOL5              Reviewed;         181 AA.
P12730; Q0TL53;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 97.
RecName: Full=S-fimbrial protein subunit SfaA;
AltName: Full=S-fimbrillin;
Flags: Precursor;
Name=sfaA; OrderedLocusNames=ECP_0293;
Escherichia coli O6:K15:H31 (strain 536 / UPEC).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=362663;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Schmoll T., Hacker J., Goebel W.;
"Nucleotide sequence of the sfaA gene coding for the S-fimbrial
protein subunit of Escherichia coli.";
FEMS Microbiol. Lett. 41:229-235(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=536 / UPEC;
PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
"Role of pathogenicity island-associated integrases in the genome
plasticity of uropathogenic Escherichia coli strain 536.";
Mol. Microbiol. 61:584-595(2006).
[3]
SUBCELLULAR LOCATION, IDENTIFICATION IN FIMBRIAE COMPLEX, AND
DISRUPTION PHENOTYPE.
PubMed=2576095; DOI=10.1111/j.1365-2958.1989.tb00159.x;
Schmoll T., Hoschuetzky H., Morschhaeuser J., Lottspeich F., Jann K.,
Hacker J.;
"Analysis of genes coding for the sialic acid-binding adhesin and two
other minor fimbrial subunits of the S-fimbrial adhesin determinant of
Escherichia coli.";
Mol. Microbiol. 3:1735-1744(1989).
-!- FUNCTION: Fimbriae (also called pili), polar filaments radiating
from the surface of the bacterium to a length of 0.5-1.5
micrometers and numbering 100-300 per cell, enable bacteria to
colonize the epithelium of specific host organs.
-!- FUNCTION: The major fimbrial subunit. Interacts with alpha-sialic
acid-(2-3)-beta-Gal containing receptors. It belongs to the group
of Mrh (Mannose-resistant hemagglutination) fimbrial proteins.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:2576095}.
-!- DISRUPTION PHENOTYPE: Deletion leads to loss of fimbriation and a
decrease of hemagglutination. {ECO:0000269|PubMed:2576095}.
-!- MISCELLANEOUS: This protein belongs to the group of SfA (S-
fimbrial adhesins), which are associated with uropathogenic
strains and with strains causing newborn meningitis.
-!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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EMBL; M35273; AAA24626.1; -; Genomic_DNA.
EMBL; X17420; CAA35468.1; -; Genomic_DNA.
EMBL; CP000247; ABG68328.1; -; Genomic_DNA.
PIR; S00352; YQECFA.
RefSeq; WP_000768216.1; NC_008253.1.
ProteinModelPortal; P12730; -.
SMR; P12730; -.
EnsemblBacteria; ABG68328; ABG68328; ECP_0293.
KEGG; ecp:ECP_0293; -.
HOGENOM; HOG000260127; -.
KO; K07345; -.
OMA; HASIIFA; -.
GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
Gene3D; 2.60.40.1090; -; 1.
InterPro; IPR008966; Adhesion_dom.
InterPro; IPR000259; Adhesion_dom_fimbrial.
InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
Pfam; PF00419; Fimbrial; 1.
SUPFAM; SSF49401; SSF49401; 1.
1: Evidence at protein level;
Disulfide bond; Fimbrium; Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 181 S-fimbrial protein subunit SfaA.
/FTId=PRO_0000009200.
DISULFID 44 84 {ECO:0000305}.
CONFLICT 55 57 VLL -> FS (in Ref. 1; AAA24626/CAA35468).
{ECO:0000305}.
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


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