ID   HTPG_THIDA              Reviewed;         633 AA.
AC   Q3SJW8;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=Tbd_1078;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97031.1; -; Genomic_DNA.
DR   RefSeq; WP_011311590.1; NC_007404.1.
DR   AlphaFoldDB; Q3SJW8; -.
DR   SMR; Q3SJW8; -.
DR   STRING; 292415.Tbd_1078; -.
DR   PRIDE; Q3SJW8; -.
DR   EnsemblBacteria; AAZ97031; AAZ97031; Tbd_1078.
DR   KEGG; tbd:Tbd_1078; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008291; 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..633
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224234"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          559..633
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   633 AA;  71167 MW;  FC0556047B54BB2C CRC64;
     MSATSSKETL GFQAEVKQLL QLMIHSLYSN KDIFLRELIS NASDAADKLR FEALSDAALF
     ENDPELKIRI AFDRDARTLT ISDNGIGMSR QEVIDHIGTI AKSGTREFFS QLSGDQKKDA
     ALIGQFGVGF YSAFIVADRV TLTTRRAGLT AEHGVRWESE GAGDYTLETV EKPQRGTEIV
     LHLREGEDEF LSDWKIKSVI RTYSDHITLP IVMKKTEWKD GVETPTDEDE TVNKASALWA
     RPKKDISDDE YNEFYKHVAH DFEPPLAWSH NRVEGKQEYI SLLYVPSHAP FDLYDREKRH
     GIKLYVRRVF IMDDAEQLMP QYLRFVRGVI DSADLPLNVS REILQSSRDI DAIKNGSVKK
     VLGMLEDLAE NQPEKYVEFW KEFGKVMKEG PGEDFANKEK IAGLLRFAST HTDTDAQVVS
     LKDYVGRMKE GQTAIYYITA DSFAAAQHSP HLEIFRKKGI EVLLLSDRVD EWLTGNLHEF
     DGKPLKSVAK GGLDLGELED EAEKTAQKEA EESMKPLVER IKAMLGERVK DVRVTHRLTD
     SPACLVTGEG DMSANLERLL KAAGQAAPTV KPTLEINPSH ALVTRLDSES DEDRFKDWAN
     LLFEQALLAE GGQLDDPASF VRRLNGLLAM LPG