ID   HTPG_COXBN              Reviewed;         633 AA.
AC   A9KGQ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=CBUD_1771;
OS   Coxiella burnetii (strain Dugway 5J108-111).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dugway 5J108-111;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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; CP000733; ABS77339.1; -; Genomic_DNA.
DR   RefSeq; WP_011997264.1; NC_009727.1.
DR   AlphaFoldDB; A9KGQ8; -.
DR   SMR; A9KGQ8; -.
DR   PRIDE; A9KGQ8; -.
DR   EnsemblBacteria; ABS77339; ABS77339; CBUD_1771.
DR   KEGG; cbd:CBUD_1771; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000008555; 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; Stress response.
FT   CHAIN           1..633
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081513"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          345..560
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          561..633
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   633 AA;  72818 MW;  5770FE52E8B76ED0 CRC64;
     MSLQPQSETL SFEAEVKQLL HLVAHSLYSN KEIFLRELIS NSSDAADKLR YQALSDAALY
     ENDADLKIWI DFDKDNRTIT IRDNGIGMSR EEVIENLGTI AKSGTRAFRE LLAEKKAEDS
     QLIGQFGVGF YSAFIVADRV VVRTRRAGMK ADQGVEWEST GEGEYTLKNI DKPTRGTEVV
     LHLKESEEEF LDPLRLRAII TKYSDHILLP IVMKKIKTSG ADDEDKNETP EEEVVNRANA
     LWVLPKDKIK DEEYKELYKH IAHDFEDPLA WVHNKVEGKL EYTTLLYIPA RAPFDIWNRE
     GQRGLKLYVK RIFIMDDAEH FMPMYLRFVK GIVDSNDLPL NISRELLQSN EVINKIKAGC
     VKRILSLLED LAKNDKEKYA SFWKAFGQVL KEGPAEDFAN RDRIANLLRF ASTHNDTDEQ
     NVSLQDYISR MKPEQNRIYY IVADTYTSAK NSPLLEVFRK KDIEVLLMSD RVDEWLVAHL
     NEFEGKSLQS IAKGTLDLGD LEKEEKVETE KFEKDFDELL KQFKEVLGEK IKDVRITHRL
     TDSPTCVVFD ENEMSGHLQR LLIQTGQDFM QAKPILEINP SHPLILRVKN ESDKTRFNRW
     ADLLLNQALL AEGEQLKDPA SFVKGLNELL LDS