(data stored in ACNUC7421 zone)

SWISSPROT: SFAG_ECOL5

ID   SFAG_ECOL5              Reviewed;         175 AA.
AC   P13429; Q0TL49;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=S-fimbrial protein subunit SfaG;
DE   Flags: Precursor;
GN   Name=sfaG; OrderedLocusNames=ECP_0297;
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], SUBCELLULAR LOCATION, IDENTIFICATION IN
RP   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).
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   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:2576095}.
CC   -!- DISRUPTION PHENOTYPE: Deletion decreases hemagglutination but no
CC       decrease in fimbriation levels. {ECO:0000269|PubMed:2576095}.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABG68332.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; X16664; CAA34652.1; -; Genomic_DNA.
DR   EMBL; CP000247; ABG68332.1; ALT_INIT; Genomic_DNA.
DR   PIR; S15925; S06193.
DR   RefSeq; WP_000237768.1; NC_008253.1.
DR   SMR; P13429; -.
DR   PRIDE; P13429; -.
DR   EnsemblBacteria; ABG68332; ABG68332; ECP_0297.
DR   KEGG; ecp:ECP_0297; -.
DR   HOGENOM; HOG000260127; -.
DR   OMA; QFYARYV; -.
DR   BioCyc; ECOL362663:G1G5S-308-MONOMER; -.
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;
DR   PRODOM; P13429.
DR   SWISS-2DPAGE; P13429.
KW   Disulfide bond; Fimbrium; Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..175
FT                   /note="S-fimbrial protein subunit SfaG"
FT                   /id="PRO_0000009201"
FT   DISULFID        43..83
FT                   /evidence="ECO:0000305"
SQ   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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