FOCC_ECOLX
ID FOCC_ECOLX Reviewed; 227 AA.
AC P62609; P46008;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Chaperone protein FocC;
DE Flags: Precursor;
GN Name=focC;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AD110 / UPEC;
RX PubMed=7836295; DOI=10.1128/jb.177.3.621-627.1995;
RA Klemm P., Joergensen B.J., Kreft B., Christiansen G.;
RT "The export systems of type 1 and F1C fimbriae are interchangeable but work
RT in parental pairs.";
RL J. Bacteriol. 177:621-627(1995).
CC -!- FUNCTION: Involved in the biogenesis of the F1C 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; Z46635; CAA86604.1; -; Genomic_DNA.
DR PIR; I41062; I41062.
DR PDB; 1L4I; X-ray; 2.20 A; A/B=22-227.
DR PDBsum; 1L4I; -.
DR AlphaFoldDB; P62609; -.
DR SMR; P62609; -.
DR PRIDE; P62609; -.
DR EvolutionaryTrace; P62609; -.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Fimbrium biogenesis; Immunoglobulin domain;
KW Periplasm; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..227
FT /note="Chaperone protein FocC"
FT /id="PRO_0000009277"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 67..90
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 102..112
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:1L4I"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1L4I"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1L4I"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1L4I"
SQ SEQUENCE 227 AA; 25199 MW; 0CDC91AFBFE5E5EF CRC64;
MRIWAVLASF LVFFYIPQSY AGVALGATRV IYPEGQKQVQ LAVTNNDDKS SYLIQSWIEN
AEGKKDARFV ITPPLFSMQG KKENTLRIID ATNGQMPEDR ESLFWVNVKA IPAMDKAKTG
ENYLQFAIVS RIKLLYRPQG LVIPPEQAPG KLEFTRENGG LTLFNPTPYY LTVTDLKAGN
KSLENTMVPP QGKVTVNIPG GYTGGDITYK TINDYGALTE QVKGVVK
