ID   FANE_ECOLX              Reviewed;         228 AA.
AC   P25402;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Chaperone protein FanE;
DE   Flags: Precursor;
GN   Name=fanE;
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].
RC   STRAIN=Isolate B41;
RX   PubMed=1713284; DOI=10.1111/j.1365-2958.1991.tb00761.x;
RA   Bakker D., Vader C.E.M., Roosendaal B., Mooi F.R., Oudega B.,
RA   de Graaf F.K.;
RT   "Structure and function of periplasmic chaperone-like proteins involved in
RT   the biosynthesis of K88 and K99 fimbriae in enterotoxigenic Escherichia
RT   coli.";
RL   Mol. Microbiol. 5:875-886(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-228.
RX   PubMed=7908067;
RA   Abe N., Moriishi K., Saito M., Naiki M.;
RT   "Confirmed nucleotide sequence of fanF of Escherichia coli K99 fimbriae.";
RL   Jpn. J. Vet. Res. 41:97-99(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-228.
RC   STRAIN=Isolate B41;
RX   PubMed=1982454; DOI=10.1111/j.1365-2958.1990.tb00564.x;
RA   Simons B.L., Willemsen P.T.J., Bakker D., Roosendaal B., de Graaf F.K.,
RA   Oudega B.;
RT   "Structure, localization and function of FanF, a minor component of K99
RT   fibrillae of enterotoxigenic Escherichia coli.";
RL   Mol. Microbiol. 4:2041-2050(1990).
CC   -!- FUNCTION: Mediates assembly of pili by forming soluble multimeric
CC       complexes with pili subunits as an intermediate step in the assembly
CC       process. This protein is involved in K99 pili assembly.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; X56001; CAA39474.1; -; Genomic_DNA.
DR   EMBL; S70131; AAB30305.1; -; Genomic_DNA.
DR   PIR; S12391; S12391.
DR   RefSeq; WP_001031857.1; NZ_VTAJ01000041.1.
DR   AlphaFoldDB; P25402; -.
DR   SMR; P25402; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Disulfide bond; Fimbrium biogenesis; Immunoglobulin domain;
KW   Periplasm; Plasmid; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..228
FT                   /note="Chaperone protein FanE"
FT                   /id="PRO_0000009271"
FT   DISULFID        157..198
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   228 AA;  25315 MW;  5F1666C15EEFB949 CRC64;
     MNKFISIIAL CVFSSYANAA FTLNSTRYIY NEGQQSVSVN IHNESEHKYG GQVWIDNIDK
     NGEVVFFSPS PMVFKLNPKQ KQIVRIVNIN DNLPKDRESI FWLNVQEIPP APKGDGGSLS
     LAINNRVKLI YRPIALKNGR DEAENNIKLI NSGTDSCLEN TTPYYFAISD VKINGKSIDL
     NSDAKNKMGV FSPFSKVCLG NVNTSGNITV TAFNDYGVAT SYTVQRSK