ID   FIMC_ECOL6              Reviewed;         241 AA.
AC   P59590;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chaperone protein FimC;
DE   Flags: Precursor;
GN   Name=fimC; OrderedLocusNames=c5395;
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: Required for the biogenesis of type 1 fimbriae. Binds and
CC       interact with FimH (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {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; AE014075; AAN83817.1; -; Genomic_DNA.
DR   RefSeq; WP_000066579.1; NC_004431.1.
DR   AlphaFoldDB; P59590; -.
DR   BMRB; P59590; -.
DR   SMR; P59590; -.
DR   STRING; 199310.c5395; -.
DR   EnsemblBacteria; AAN83817; AAN83817; c5395.
DR   KEGG; ecc:c5395; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_2_1_6; -.
DR   OMA; LFAMQGK; -.
DR   BioCyc; ECOL199310:C5395-MON; -.
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..36
FT                   /evidence="ECO:0000250"
FT   CHAIN           37..241
FT                   /note="Chaperone protein FimC"
FT                   /id="PRO_0000009274"
SQ   SEQUENCE   241 AA;  26597 MW;  701811F8458FD4C0 CRC64;
     MSNKNVNVRK SQEITFCLLA GILMFMAMVV AGRAEAGVAL GATRVIYPAG QKQVQLAVTN
     NDENSTYLIQ SWVENADGVK DGRFIVTPPL FAMKGKKENT LRILDATNNQ LPQDRESLFW
     MNVKAIPSMD KSKLTENTLQ LAIISRIKLY YRPAKLALPP DQAAEKLRFR RSANSLTLIN
     PTPYYLTVTE LNAGTRVLEN ALVPPMGESA VKLPSDAGSN ITYRTINDYG ALTPKMTGVM
     E