GENTAUR Molecular Products.

 SFAG_ECOL5              Reviewed;         175 AA.
 P13429; Q0TL49;
 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
 01-JAN-1990, sequence version 1.
 22-NOV-2017, entry version 99.
 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; IPR000259; Adhesion_dom_fimbrial.
 InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
 InterPro; IPR008966; Adhesion_dom_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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