FAED_ECOLX
ID FAED_ECOLX Reviewed; 812 AA.
AC P06970;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Outer membrane usher protein FaeD;
DE Flags: Precursor;
GN Name=faeD;
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=2870470; DOI=10.1093/nar/14.6.2443;
RA Mooi F.R., Claassen I., Bakker D., Kuipers H., de Graaf F.K.;
RT "Regulation and structure of an Escherichia coli gene coding for an outer
RT membrane protein involved in export of K88ab fimbrial subunits.";
RL Nucleic Acids Res. 14:2443-2457(1986).
RN [2]
RP SEQUENCE REVISION.
RA Oudega B.;
RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8577257; DOI=10.1111/j.1365-2958.1995.tb02346.x;
RA Valent Q.A., Zaal J., de Graaf F.K., Oudega B.;
RT "Subcellular localization and topology of the K88 usher FaeD in Escherichia
RT coli.";
RL Mol. Microbiol. 16:1243-1257(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 794-812.
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 K88ab fimbrial
CC subunits 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; X03675; CAA27310.1; -; Genomic_DNA.
DR EMBL; X56002; CAA39476.1; -; Genomic_DNA.
DR EMBL; X56003; CAA39477.1; -; Genomic_DNA.
DR PIR; S24931; MMECOF.
DR AlphaFoldDB; P06970; -.
DR SMR; P06970; -.
DR TCDB; 1.B.11.1.1; the outer membrane fimbrial usher porin (fup) family.
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..35
FT CHAIN 36..812
FT /note="Outer membrane usher protein FaeD"
FT /id="PRO_0000009308"
FT DISULFID 793..811
FT /evidence="ECO:0000255"
SQ SEQUENCE 812 AA; 85497 MW; C6DAACA4AD88DAFC CRC64;
MKKYVTTKSV QPVAFRLTTL SLVMSAVLGS ASVIAGEKLD MSFIQGGGGV NPEVWAALNG
SYAPGRYLVD LSLNGKEAGK QILDVTPQDS NELCLTEAWL TKAGVYVSAD YFREGYDATR
QCYVLTKAPS VKVDFDVSTQ SLALSIPQKG LVKMPENVDW DYGTSAFRVN YNANANTGRN
NTSAFGSADL KANIGHWVVS SSATASGGDS GDNSTTINMF TATRAIRALS ADLAVGKTST
GDSLLGSTGT YGVSLSRNNS MKPGNLGYTP VFSGIANGPS RVTLTQNGRL LHSEMVPAGP
FSITDVPLYT SGDVTMKITG EDGRDEVQNF PLSVMAGQLS PGQHEFSVAA GLPDDDSDLK
GGVFAASYGY GLDGLTLRAG GVFNQDWQGA SAGVVAGLGY LGAVSADGAY ATAKYRDGSH
SGNKVQLSWS KQLETTNTGL RVSWSRQSEE YEGMSSFDPT ELWSQSNHGR RTKDEWNAGI
SQPVGGLFSL SVSGWQRSYY PASMTGSYRY SDDNGKETGI TGSLSTQIKG VSLNLGWSGS
RNSRGENNWS ASASVSVPFT LFDRRYSSSA SVSTSKGGGT GFSTGVSGSL NDRFSYGLGG
GRDGDGGTSS YLNASYSGDR AYLNGVLNHS QSGGTSGSVS VSGSVLAVPA AKDIMFSRTT
GDTVAVVNVK DTPGVKVTSG DGQTDSDGNL VVPLNSYDWN TVTIDTGTLP LSTELTNTSQ
KVVPTDKAVV WMPFDALKVK RYLLQVKQRD GEFVPGGTWA RDSKNTPLGF VANNGVLMIN
TVDAPGDITL GQCRIPAARL QDTEKLQEIT CE