FAEE_ECOLX
ID FAEE_ECOLX Reviewed; 258 AA.
AC P25401;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Chaperone protein FaeE;
DE Flags: Precursor;
GN Name=faeE;
OS Escherichia coli.
OG Plasmid pFM205.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1713284; DOI=10.1111/j.1365-2958.1991.tb00761.x;
RA Bakker D., Vader C.E.M., Roosendaal B., Mooi F.R., Oudega B.,
RA de Graaf F.K.;
RT "Structure and function of periplasmic chaperone-like proteins involved in
RT the biosynthesis of K88 and K99 fimbriae in enterotoxigenic Escherichia
RT coli.";
RL Mol. Microbiol. 5:875-886(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-258.
RX PubMed=1400188; DOI=10.1128/jb.174.20.6350-6358.1992;
RA Bakker D., Willemsen P.T.J., Willems R.H., Huisman T.T., Mooi F.R.,
RA Oudega B., Stegehuis F., de Graaf F.K.;
RT "Identification of minor fimbrial subunits involved in biosynthesis of K88
RT fimbriae.";
RL J. Bacteriol. 174:6350-6358(1992).
CC -!- FUNCTION: Mediates assembly of pili by forming soluble multimeric
CC complexes with pili subunits as an intermediate step in the assembly
CC process. This protein is involved in K88 pili assembly. Protects pilin
CC protein from proteolytic degradation by DegP and from premature
CC polymerization.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC {ECO:0000305}.
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DR EMBL; X56003; CAA39478.1; -; Genomic_DNA.
DR EMBL; Z11699; CAA77756.1; -; Genomic_DNA.
DR PIR; S15227; S15227.
DR RefSeq; WP_000044493.1; NZ_QZWA01000069.1.
DR PDB; 3F65; X-ray; 2.29 A; A/B/C/D/E/F/G/H=35-258.
DR PDB; 3F6I; X-ray; 2.79 A; A/B=35-258.
DR PDB; 3F6L; X-ray; 2.80 A; A/B=35-258.
DR PDB; 3GEW; X-ray; 2.00 A; B/C=35-258.
DR PDB; 3GFU; X-ray; 1.99 A; A/C=35-258.
DR PDBsum; 3F65; -.
DR PDBsum; 3F6I; -.
DR PDBsum; 3F6L; -.
DR PDBsum; 3GEW; -.
DR PDBsum; 3GFU; -.
DR AlphaFoldDB; P25401; -.
DR SMR; P25401; -.
DR EvolutionaryTrace; P25401; -.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Fimbrium biogenesis; Immunoglobulin domain;
KW Periplasm; Plasmid; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..258
FT /note="Chaperone protein FaeE"
FT /id="PRO_0000009270"
FT REGION 239..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3F65"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3F6L"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 135..146
FT /evidence="ECO:0007829|PDB:3GFU"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3GFU"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3F6L"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:3GFU"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:3GFU"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3GFU"
SQ SEQUENCE 258 AA; 28478 MW; FF80904B3DE5420B CRC64;
MSKRNAVTTF FTNRVTKALG MTLALMMTCQ SAMASLAVDQ TRYIFRGDKD ALTITVTNND
KERTFGGQAW VDNIVEKDTR PTFVVTPSFF KVKPNGQQTL RIIMASDHLP KDKESVYWLN
LQDIPPALEG SGIAVALRTK LKLFYRPKAL LEGRKGAEEG ISLQSRPDGR TMLVNTTPYI
FAIGSLLDGN GKKIATDNGT TQKLLMFMPG DEVQVKGNVV KVDSLNDYGE LQTWTINKKK
PAAPEAAKAE KADTAEQK
