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FIMB_BORPE
ID   FIMB_BORPE              Reviewed;         244 AA.
AC   P33409;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Chaperone protein FimB/FhaD;
DE   Flags: Precursor;
GN   Name=fimB; Synonyms=fhaD; OrderedLocusNames=BP1881;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wellcome 28;
RX   PubMed=1360139; DOI=10.1111/j.1365-2958.1992.tb01443.x;
RA   Willems R.J.L., van der Heide H.G.J., Mooi F.R.;
RT   "Characterization of a Bordetella pertussis fimbrial gene cluster which is
RT   located directly downstream of the filamentous haemagglutinin gene.";
RL   Mol. Microbiol. 6:2661-2671(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=1354611; DOI=10.1002/j.1460-2075.1992.tb05394.x;
RA   Locht C., Geoffroy M.C., Renauld G.;
RT   "Common accessory genes for the Bordetella pertussis filamentous
RT   hemagglutinin and fimbriae share sequence similarities with the papC and
RT   papD gene families.";
RL   EMBO J. 11:3175-3183(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Required for the biogenesis of the filamentous hemagglutinin
CC       and the fimbria.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; X64876; CAA46089.1; -; Genomic_DNA.
DR   EMBL; X66729; CAA47265.1; -; Genomic_DNA.
DR   EMBL; BX640416; CAE42164.1; -; Genomic_DNA.
DR   PIR; S36245; S36245.
DR   RefSeq; NP_880572.1; NC_002929.2.
DR   RefSeq; WP_010930611.1; NZ_CP039022.1.
DR   AlphaFoldDB; P33409; -.
DR   SMR; P33409; -.
DR   STRING; 257313.BP1881; -.
DR   GeneID; 45389212; -.
DR   KEGG; bpe:BP1881; -.
DR   PATRIC; fig|257313.5.peg.2019; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_0_2_4; -.
DR   OMA; AWIDNGN; -.
DR   Proteomes; UP000002676; Chromosome.
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; Fimbrium biogenesis; Immunoglobulin domain; Periplasm;
KW   Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..244
FT                   /note="Chaperone protein FimB/FhaD"
FT                   /id="PRO_0000009272"
FT   CONFLICT        27
FT                   /note="A -> D (in Ref. 1; CAA46089)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  26436 MW;  B2E82131C355DCD9 CRC64;
     MARWRRRLGV AALGAAMLAS LAPAARASLV ITGTRVIYNA GSPETTVKMS NEGQAPALMQ
     AWIDDGNAEA KPDEVQVPFF LTPPLARVDP GKGQTLRIFF NGYPDGKTLP SDRESVFWLN
     VLEVPPKATP EEGHGVLQLT IRSRLKLFYR PKGLSGNPLT AAADLTFKRK PNGVLEVHNP
     TPYYVNLQKL EVGENGAHGS KTPWMLAPLS SDELRLKGTG AKSVQYWAID DFGGVTPYQA
     AIAD
 
 
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