ID   AGGD_ECOLX              Reviewed;         252 AA.
AC   P46004;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Chaperone protein AggD;
DE   Flags: Precursor;
GN   Name=aggD;
OS   Escherichia coli.
OG   Plasmid P17-2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O3:H2 / 17-2 / EAggEC;
RX   PubMed=7914189; DOI=10.1128/jb.176.16.4949-4957.1994;
RA   Savarino S.J., Fox P., Deng Y., Nataro J.P.;
RT   "Identification and characterization of a gene cluster mediating
RT   enteroaggregative Escherichia coli aggregative adherence fimbria I
RT   biogenesis.";
RL   J. Bacteriol. 176:4949-4957(1994).
CC   -!- FUNCTION: Involved in the biogenesis of the AAF/I fimbriae.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; U12894; AAA57451.1; -; Genomic_DNA.
DR   PIR; A55853; A55853.
DR   RefSeq; WP_032154288.1; NZ_WNTS01000037.1.
DR   AlphaFoldDB; P46004; -.
DR   SMR; P46004; -.
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; Plasmid;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..252
FT                   /note="Chaperone protein AggD"
FT                   /id="PRO_0000009263"
SQ   SEQUENCE   252 AA;  28161 MW;  D88373585096A985 CRC64;
     MKIRRIVSTI AIALSVFTFA HAQSFENVEN NAKVFSLHLG ATRMIYKPNS SGETLAVINE
     HNYPILVQAN VLSEDQKNIA PFIITPPLFR LDALQSSRLR IVKTEGAFPI DRESLQWICV
     KAIPPKYEDK WAKEEVSGKK SDKATMNIQV SVSSCIKLFV RPADVKGQPD DVAGKIKWQK
     VGNKLKGVNP TPFYMDIAEL RVGEKEITET HYIAPFSSYE YPMPVNGGGD VRWKVVTDYG
     GISKTFETGL NI