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NFAE_ECOLX
ID   NFAE_ECOLX              Reviewed;         247 AA.
AC   P46738;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Chaperone protein NfaE;
DE   Flags: Precursor;
GN   Name=nfaE;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O83:K1:H4 / 827 / UPEC;
RX   PubMed=8099066; DOI=10.1128/iai.61.6.2505-2512.1993;
RA   Ahrens R., Ott M., Ritter A., Hoschuetzky H., Buehler T., Lottspeich F.,
RA   Boulnois G.J., Jann K., Hacker J.;
RT   "Genetic analysis of the gene cluster encoding nonfimbrial adhesin I from
RT   an Escherichia coli uropathogen.";
RL   Infect. Immun. 61:2505-2512(1993).
CC   -!- FUNCTION: Involved in the biogenesis of the NFA-I adhesin.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; S61968; AAB26855.2; -; Genomic_DNA.
DR   AlphaFoldDB; P46738; -.
DR   SMR; P46738; -.
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   3: Inferred from homology;
KW   Chaperone; Immunoglobulin domain; Periplasm; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..247
FT                   /note="Chaperone protein NfaE"
FT                   /id="PRO_0000009284"
FT   REGION          105..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  27049 MW;  6F32A5B905568516 CRC64;
     MKMRAVAVFT GMLTGVLSVT GLLSAGAYAA GGEGNMSASA TETNARVFSL HLGATRVVYN
     PASSGETLTV INDQDYPMLV QSEVLSEDQK SPAPFWWTPP LFRRDGQQSS RRRSVSTGGE
     FPSDRESRQW ICVKGIPPKE DDRWAEGKDG EKKADKVSLN VQLSVSSCIK LFVRPPAVKG
     RPDDVAGKVE WQRAGNRLKG VNPTPFYINL STLTVGGKEV KEREYIAPFS SREYPLPAGH
     RVRFSGR
 
 
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