ID   FOCC_ECOL6              Reviewed;         227 AA.
AC   P62610; P46008;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Chaperone protein FocC;
DE   Flags: Precursor;
GN   Name=focC; OrderedLocusNames=c1241;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Involved in the biogenesis of the F1C fimbriae.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79698.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79698.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P62610; -.
DR   SMR; P62610; -.
DR   STRING; 199310.c1241; -.
DR   EnsemblBacteria; AAN79698; AAN79698; c1241.
DR   KEGG; ecc:c1241; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_2_1_6; -.
DR   OMA; YLINAWI; -.
DR   Proteomes; UP000001410; Chromosome.
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; Fimbrium biogenesis; Immunoglobulin domain; Periplasm; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..227
FT                   /note="Chaperone protein FocC"
FT                   /id="PRO_0000009278"
SQ   SEQUENCE   227 AA;  25199 MW;  0CDC91AFBFE5E5EF CRC64;
     MRIWAVLASF LVFFYIPQSY AGVALGATRV IYPEGQKQVQ LAVTNNDDKS SYLIQSWIEN
     AEGKKDARFV ITPPLFSMQG KKENTLRIID ATNGQMPEDR ESLFWVNVKA IPAMDKAKTG
     ENYLQFAIVS RIKLLYRPQG LVIPPEQAPG KLEFTRENGG LTLFNPTPYY LTVTDLKAGN
     KSLENTMVPP QGKVTVNIPG GYTGGDITYK TINDYGALTE QVKGVVK