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 25-MAY-2022, entry version 111.
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};
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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 AlphaFoldDB; P13429; -.
DR SMR; P13429; -.
DR STRING; 362663.ECP_0297; -.
DR EnsemblBacteria; ABG68332; ABG68332; ECP_0297.
DR KEGG; ecp:ECP_0297; -.
DR HOGENOM; CLU_088965_0_2_6; -.
DR OMA; QFYARYV; -.
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 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
