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S-fimbrial protein subunit SfaG

 SFAG_ECOL5              Reviewed;         175 AA.
P13429; Q0TL49;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-OCT-2017, entry version 98.
RecName: Full=S-fimbrial protein subunit SfaG;
Flags: Precursor;
Name=sfaG; OrderedLocusNames=ECP_0297;
Escherichia coli O6:K15:H31 (strain 536 / UPEC).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=362663;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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).
[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).
-!- 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: A minor fimbrial subunit. This protein is necessary for
full expression of S-specific binding. S-fimbrial adhesins enable
pathogenic E.coli causing urinary-tract infections or newborn
meningitis to attach to glycoproteins terminating with alpha-
sialic acid-(2-3)-beta-Gal.
-!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:2576095}.
-!- DISRUPTION PHENOTYPE: Deletion decreases hemagglutination but no
decrease in fimbriation levels. {ECO:0000269|PubMed:2576095}.
-!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABG68332.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X16664; CAA34652.1; -; Genomic_DNA.
EMBL; CP000247; ABG68332.1; ALT_INIT; Genomic_DNA.
PIR; S15925; S06193.
RefSeq; WP_000237768.1; NC_008253.1.
ProteinModelPortal; P13429; -.
SMR; P13429; -.
EnsemblBacteria; ABG68332; ABG68332; ECP_0297.
KEGG; ecp:ECP_0297; -.
HOGENOM; HOG000260127; -.
OMA; QFYARYV; -.
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 27
CHAIN 28 175 S-fimbrial protein subunit SfaG.
/FTId=PRO_0000009201.
DISULFID 43 83 {ECO:0000305}.
SEQUENCE 175 AA; 18581 MW; 38F3E13CA57B0629 CRC64;
MVKDIIKTVT FSCMLAGSMF VTCHVCAAGS VVNITGNVQD NTCDVDINSR NFDVSLGSYD
SRQFTAAGDT TPASVFHVGL TSCGSAVRAV KLTFTGTPDN QEAGLIQINS INGARGVGIQ
LLDKDKHELK INVPTTIALM PGTQTIAFYA RLKATYLPVK AGNVDAVVNF VLDYQ


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