ID   CSSC1_ECOLX             Reviewed;         232 AA.
AC   P53518;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Chaperone protein CssC;
DE   Flags: Precursor;
GN   Name=cssC;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O167:H5 / E10703 / EIEC;
RA   Wolf M.K., de Haan L., Cassels F.C., Willshaw G.A., van Gestel E.,
RA   Gaastra W., Warren R., Boedeker E.C.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biogenesis of the CS6 fimbria.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
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; U04844; AAC45095.1; -; Unassigned_DNA.
DR   PIR; I83349; I83349.
DR   AlphaFoldDB; P53518; -.
DR   SMR; P53518; -.
DR   PRIDE; P53518; -.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..232
FT                   /note="Chaperone protein CssC"
FT                   /id="PRO_0000009267"
SQ   SEQUENCE   232 AA;  26832 MW;  234939C04B872925 CRC64;
     MKSKLIILLM LVPFSSFSTE NNFEINKTRV IYSDSTPSVQ ISNNKAYPLI VQSNIWDENN
     NKNHDFIATP PIFKMESESR NIIKIIKTNI KLPDSQESMR WLCIESMPPT EKSTKINRKE
     GRTDSINISI RGCIKLIYQP ASVPSPVFNN IVEKLKWHKN GKYLVLKNNT PYYISFSEVF
     FDSDKVNNAK DILYVKPYSE KKIDISNRII KKIKWAMIDD AGAKTKLYES IL