ID   CLPE_ECOLX              Reviewed;         263 AA.
AC   Q05433;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Chaperone protein ClpE;
DE   Flags: Precursor;
GN   Name=clpE;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8097176; DOI=10.1016/0378-1097(93)90488-n;
RA   Bertin Y., Girardeau J.P., der Vartanian M., Martin C.;
RT   "The ClpE protein involved in biogenesis of the CS31A capsule-like antigen
RT   is a member of a periplasmic chaperone family in Gram-negative bacteria.";
RL   FEMS Microbiol. Lett. 108:59-68(1993).
CC   -!- FUNCTION: Involved in the biogenesis of the CS31A capsule-like antigen.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; L05180; AAA23598.1; -; Genomic_DNA.
DR   PIR; I41172; I41172.
DR   AlphaFoldDB; Q05433; -.
DR   SMR; Q05433; -.
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; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
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; Immunoglobulin domain; Periplasm; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..263
FT                   /note="Chaperone protein ClpE"
FT                   /id="PRO_0000009265"
FT   REGION          238..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  29041 MW;  8C823FE9681B9DF1 CRC64;
     MSKRNAVTTF FTNRVTKALG MTLALMMTCQ SAMASLAADQ TRYIFRGDKD ALTITVTNND
     KERTFGGQAW VDNIVEKDTR PTFVVTPSFF KVKPNGQQTL RIIMASDHLP KDKESVYWLN
     LQDIPPALEG SGIAVAVRTK LKLFYRPKAL IEGRKGAEEG ISLQSRPDGR TMLVNTTPYI
     FAIGSLLDGN GKRIATDNET AQKLLMFMPG DEVQVKGNVV KVDSLNDYGE LQTWTINQKK
     TPTSSGQKAS DSLVNPSDKA DKK