ID   CS31_ECOLX              Reviewed;         241 AA.
AC   P15483;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Chaperone protein CS3-1;
DE   Flags: Precursor;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PB176 / ETEC;
RX   PubMed=2576094; DOI=10.1111/j.1365-2958.1989.tb00154.x;
RA   Jalajakumari M.B., Thomas C.J., Halter R., Manning P.A.;
RT   "Genes for biosynthesis and assembly of CS3 pili of CFA/II enterotoxigenic
RT   Escherichia coli: novel regulation of pilus production by bypassing an
RT   amber codon.";
RL   Mol. Microbiol. 3:1685-1695(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RX   PubMed=2903130; DOI=10.1128/iai.56.12.3297-3300.1988;
RA   Boylan M., Smyth C.J., Scott J.R.;
RT   "Nucleotide sequence of the gene encoding the major subunit of CS3 fimbriae
RT   of enterotoxigenic Escherichia coli.";
RL   Infect. Immun. 56:3297-3300(1988).
CC   -!- FUNCTION: This protein is essential for the biogenesis of mature CS3
CC       pili.
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; X16944; CAA34815.1; -; Genomic_DNA.
DR   EMBL; M35657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S07899; S07899.
DR   AlphaFoldDB; P15483; -.
DR   SMR; P15483; -.
DR   PRIDE; P15483; -.
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; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..241
FT                   /note="Chaperone protein CS3-1"
FT                   /id="PRO_0000009266"
FT   DISULFID        113..144
FT                   /evidence="ECO:0000255"
FT   CONFLICT        73
FT                   /note="N -> S (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   241 AA;  26908 MW;  DBC9767D163FCFA0 CRC64;
     MTPIKLIFAA LSLFPCSNIY ANNITTQKFE AILGATRVIY HLDGNGESLR VKNPQISPIL
     IQSKVMDEGS KDNADFIVTP PLFRLDAKRE TDIRIVMVNG LYPKDRESLK TLCVRGIPPK
     QGDLWANNEK EFVGMKLNVS INTCIKLILR PHNLPKLDIN SEGQIEWGIR DGNLVAKNKT
     PYYFTIVNAS FNGKALKTPG TLGPYEQKLY TLPSKISVSG LVKWEIIGDL GESSETKKFN
     I