ID   FANC_ECOLX              Reviewed;         181 AA.
AC   P18103;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=K99 fimbrial protein;
DE   Flags: Precursor;
GN   Name=fanC;
OS   Escherichia coli.
OG   Plasmid pFK99.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Roosendaal B., Gaastra W., de Graaf F.K.;
RT   "The nucleotide sequence of the gene encoding the K99 subunit of
RT   enterotoxigenic Escherichia coli.";
RL   FEMS Microbiol. Lett. 22:253-258(1984).
RN   [2]
RP   IMPORTANCE OF RESIDUE 180.
RX   PubMed=1970318; DOI=10.1016/0378-1097(90)90177-r;
RA   Simons B.L., Rathman P., Maij C.R., Oudega B., de Graaf F.K.;
RT   "The penultimate tyrosine residue of the K99 fibrillar subunit is essential
RT   for stability of the protein and its interaction with the periplasmic
RT   carrier protein.";
RL   FEMS Microbiol. Lett. 55:107-112(1990).
RN   [3]
RP   IMPORTANCE OF RESIDUES 154 AND 158.
RX   PubMed=2886335; DOI=10.1002/j.1460-2075.1987.tb02434.x;
RA   Jacobs A.A.C., Simons L.H., de Graaf F.K.;
RT   "The role of lysine-132 and arginine-136 in the receptor-binding domain of
RT   the K99 fibrillar subunit.";
RL   EMBO J. 6:1805-1808(1987).
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: FanC is the main component of the K99 fimbriae.
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35282; AAA24037.1; -; Genomic_DNA.
DR   PIR; I41321; I41321.
DR   AlphaFoldDB; P18103; -.
DR   SMR; P18103; -.
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; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Fimbrium; Plasmid; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..181
FT                   /note="K99 fimbrial protein"
FT                   /id="PRO_0000009203"
FT   SITE            154
FT                   /note="Required for receptor binding"
FT   SITE            158
FT                   /note="Required for receptor binding"
FT   SITE            180
FT                   /note="Required for stability and transport"
FT   DISULFID        38..79
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   181 AA;  18738 MW;  2BDF3E792809790F CRC64;
     MKKTLLAIIL GGMAFATTNA SANTGTINFN GKITSATCTI DPEVNGNRTS TIDLGQAAIS
     GHGTVVDFKL KPAPGSNDCL AKTNARIDWS GSMNSLGFNN TASGNTAAKG YHMTLRATNV
     GNGSGGANIN TSFTTAEYTH TSAIQSFNYS AQLKKDDRAP SNGGYKAGVF TTSASFLVTY
     M