位置:首页 > 蛋白库 > HTPG_BORPE
HTPG_BORPE
ID   HTPG_BORPE              Reviewed;         635 AA.
AC   Q7W0M8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=BP0074;
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 [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: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX640411; CAE40453.1; -; Genomic_DNA.
DR   RefSeq; NP_878979.1; NC_002929.2.
DR   RefSeq; WP_010929604.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7W0M8; -.
DR   SMR; Q7W0M8; -.
DR   STRING; 257313.BP0074; -.
DR   GeneID; 45390720; -.
DR   KEGG; bpe:BP0074; -.
DR   PATRIC; fig|257313.5.peg.73; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..635
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062973"
FT   REGION          1..346
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          347..563
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          564..635
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   635 AA;  71154 MW;  63C8EC8663A523C0 CRC64;
     MSQTTTTSAS ETLGFQAEVK QLLHLMIHSL YSNKEIFLRE LVSNASDACD KLRFEAIDQP
     GLLEGDGELA IRVGYDKAAR TITISDNGIG LSRDEAVANL GTIARSGTRE FFSQLTGDKQ
     KDAQLIGQFG VGFYSSFIVA DKVTVLSRRA GLAANEAIRW ESDGQGEFSI APAEKAGRGT
     DVVLHLRADE DELLNGWKLR EILRRYSDHI SLPIRMAKED WDAEKGEQVK GDELETVNQA
     NALWTRNKSD ITDEQYREFY KTVSHDYDDP LAWTHNRVEG RSEYTQLLYV PKHAPFDLWD
     RDARRGVKLY VKRVFIMDDA EQLLPSYLRF VRGVIDSADL PLNVSREILQ ESRDVRAIRE
     GSAKRVLSLL EDMAENKAED YATFWTEFGQ VLKEGTGEDA ANRERIARLL RFASTHDGEQ
     AQTVSFADYV GRMKDGQDKI YYVTADTFTA AANSPHLEIF RKKGIEVLLL SDRVDEWMLS
     YLREFDGKSL VSVAKGGLDL AELADEEEKK RQSEVAETFK PLVERLQQAL AEQVKEVRVT
     QRLVDSPACV VVGQNELSPH LLRMLKAAGQ EAPEVKPVLE INPDHALVAR IRDASDAEFG
     DWAALLLDQA LLAEGAQIAD PAAFVKRLNG LLLKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024