FAEG3_ECOLX
ID FAEG3_ECOLX Reviewed; 285 AA.
AC P14191;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=K88 fimbrial protein AD;
DE AltName: Full=K88 antigen;
DE AltName: Full=K88 pilin;
DE Flags: Precursor;
GN Name=faeG;
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=2412961; DOI=10.1128/iai.50.1.279-283.1985;
RA Dykes C.W., Halliday I.J., Read M.J., Hobden A.N., Harford S.;
RT "Nucleotide sequences of four variants of the K88 gene of porcine
RT enterotoxigenic Escherichia coli.";
RL Infect. Immun. 50:279-283(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-275.
RA Gaastra W., Klemm P., de Graaf F.K.;
RT "The nucleotide sequence of the K88ad protein subunit of porcine
RT enterotoxigenic Escherichia coli.";
RL FEMS Microbiol. Lett. 18:177-183(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51 AND 272-285.
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: K88 major fimbrial subunit. Fimbriae (also called pili), are
CC polar filaments radiating from the surface of the bacterium to a length
CC of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable
CC bacteria to colonize the epithelium of specific host organs.
CC -!- SUBUNIT: K88 fimbria, 0.1-1 micrometer in length and 7 nanometers in
CC diameter, is composed of about 100 identical subunits.
CC -!- SUBCELLULAR LOCATION: Fimbrium.
CC -!- MISCELLANEOUS: The protein exists in several antigenic variants.
CC -!- SIMILARITY: Belongs to the fimbrial K88 protein family. {ECO:0000305}.
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DR EMBL; M29376; AAA24035.1; -; Genomic_DNA.
DR EMBL; M35637; AAA24036.1; -; Genomic_DNA.
DR EMBL; Z11699; CAA77758.1; -; Genomic_DNA.
DR EMBL; Z11700; CAA77759.1; -; Genomic_DNA.
DR EMBL; Z11710; CAA77770.1; -; Genomic_DNA.
DR PIR; I41319; I41319.
DR PDB; 3GEA; X-ray; 1.70 A; A/B=43-285.
DR PDB; 3GEW; X-ray; 2.00 A; A/D=43-285.
DR PDB; 3GGH; X-ray; 1.64 A; A/B=43-285.
DR PDB; 3HLR; X-ray; 2.30 A; A=22-285.
DR PDB; 4WEI; X-ray; 2.30 A; A=40-285.
DR PDB; 4WEU; X-ray; 2.61 A; A/B=40-285.
DR PDBsum; 3GEA; -.
DR PDBsum; 3GEW; -.
DR PDBsum; 3GGH; -.
DR PDBsum; 3HLR; -.
DR PDBsum; 4WEI; -.
DR PDBsum; 4WEU; -.
DR AlphaFoldDB; P14191; -.
DR SMR; P14191; -.
DR UniLectin; P14191; -.
DR EvolutionaryTrace; P14191; -.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Fimbrium; Plasmid; Signal.
FT SIGNAL 1..21
FT CHAIN 22..285
FT /note="K88 fimbrial protein AD"
FT /id="PRO_0000009196"
FT CONFLICT 59
FT /note="N -> S (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="K -> E (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="I -> S (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="K -> R (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..96
FT /note="TS -> VG (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="T -> I (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="K -> Q (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="E -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="K -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="G -> R (in Ref. 2; AAA24036)"
FT /evidence="ECO:0000305"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3GGH"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3GGH"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:3GGH"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3HLR"
FT STRAND 141..158
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:3GGH"
FT TURN 178..182
FT /evidence="ECO:0007829|PDB:4WEI"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:3GGH"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:3GGH"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3HLR"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3GGH"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:3GGH"
SQ SEQUENCE 285 AA; 29602 MW; FBEF2F57910D91ED CRC64;
MKKTLIALAI AASAASGMAH AWMTGDFNGS VDIGGSITAD DYRQKWEWKV GTGLNGFGNV
LNDLTNGGTK LTITVTGNKP ILLGRTKEAF ATPVTSGVDG IPHIAFTDYE GASVELRNPD
GETEKGLAYF VLPMKNAEGT KVGSVKVNAS YAGALGRGGV TSADGELMSL FAEGSHAIFY
GGLPTNVKNS ELKGGSAAAA RTELFGSLSK NDILGQIQRV NANITSLVNV PGSFNENMAY
TDGSVVSVAY ALGIANGQTI EATFNQAVTT STQWSAPLNV AITYY
