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}.
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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