FAND_ECOLX
ID FAND_ECOLX Reviewed; 783 AA.
AC P12050;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Outer membrane usher protein FanD;
DE Flags: Precursor;
GN Name=fanD;
OS Escherichia coli.
OG Plasmid pFK99.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B41;
RX PubMed=2564179; DOI=10.1093/nar/17.3.1263;
RA Roosendaal B., Bakker D., de Graaf F.K.;
RT "The nucleotide sequence of the fanD gene encoding the large outer membrane
RT protein involved in the biosynthesis of K99 fimbriae.";
RL Nucleic Acids Res. 17:1263-1263(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RA Roosendaal B., Gaastra W., de Graaf F.K.;
RT "The nucleotide sequence of the gene encoding the K99 subunit of
RT enterotoxigenic Escherichia coli.";
RL FEMS Microbiol. Lett. 22:253-258(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 770-783.
RC STRAIN=B41;
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).
CC -!- FUNCTION: Involved in the export and assembly of K99 fimbrial subunits
CC across the outer membrane.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fimbrial export usher family. {ECO:0000305}.
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DR EMBL; X13560; CAA31911.1; -; Genomic_DNA.
DR EMBL; M35282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X56001; CAA39473.1; -; Genomic_DNA.
DR PIR; S02755; S02755.
DR AlphaFoldDB; P12050; -.
DR SMR; P12050; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015473; F:fimbrial usher porin activity; IEA:InterPro.
DR GO; GO:0009297; P:pilus assembly; IEA:InterPro.
DR Gene3D; 2.60.40.2610; -; 1.
DR Gene3D; 3.10.20.410; -; 1.
DR InterPro; IPR000015; Fimb_usher.
DR InterPro; IPR018030; Fimbrial_membr_usher_CS.
DR InterPro; IPR042186; FimD_plug_dom.
DR InterPro; IPR025885; PapC_N.
DR InterPro; IPR037224; PapC_N_sf.
DR PANTHER; PTHR30451; PTHR30451; 1.
DR Pfam; PF13954; PapC_N; 1.
DR Pfam; PF00577; Usher; 1.
DR SUPFAM; SSF141729; SSF141729; 1.
DR PROSITE; PS01151; FIMBRIAL_USHER; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Disulfide bond; Fimbrium biogenesis; Membrane;
KW Plasmid; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..783
FT /note="Outer membrane usher protein FanD"
FT /id="PRO_0000009309"
FT DISULFID 763..782
FT /evidence="ECO:0000255"
SQ SEQUENCE 783 AA; 87157 MW; 23BDE3923A9B7069 CRC64;
MNRKKHQILK ILLLCLISSK SSASEKELNL QFIRHKFGQN TEDIELFFNS STVLPGNYTV
DVKLNDEVIG RAKLEVSQDD KESYCLKDEW LSDLGIIINR DFYNKYFNIK RECYEIGKEK
NSITTFDNNS QIFSLYMPQA AYIKKGNTEH KWSYGDPGFN LNYDAYLSKN DEDSSIYGNL
EGNVNIDKWV LYGRGYKYEH DKFTTDDVTL SRAIKSLEGD LIIGDTYTNT SLMDNISFYG
VQLRSNNAMT PERRGDYSPI ISGIAKSNAR VTVKQNGVVL HSELVSPGPF HINNVRGIRS
GELVMTVTEE DGSEQQTRIP VTFIANLLSP GNYNYDFGIG NKEATWEPDN IFAYGSFDYG
LNLLTLNASL LFEQHYSNAG IGAVGSIGSL GAVSVSGNIS RAKNQLETDQ GYSTSANYSK
NVGANGNLQI IGYKFSSEGY TQYANFDYRA PRKDKKEKER YEVTLTQQFP ASNVFLSVTG
WKKFYWNDNS VTGANVSYTQ NFGTVNASVN GSYSRGDGAK SDYMLGFNIN IPFRHNDRQF
YSNSGVTYNR NSGIGFNAGF SEDVTKNFNY NVNAAASKDN ESVSLSTNYT SSMFRTSASV
SKNRNSTNAS AQIGGAIIGV KDGGVMLTSM SSNSVAIVQM EGLAGYAFTN GVESDWRGRI
AYPMTTYMDN DIQISTDKLP SNIELTDNVE TIVPTNRAIK LQKIKYKNMS RHVLKVYDKN
GFVIPMGTAV KNSNGEIISF VNNNGISLLN IDKNDERVFF GSCTISTSGL KDNLSEIQEV
NCE