ID   HTPG_ALKHC              Reviewed;         625 AA.
AC   Q9KE51;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=BH1007;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB04726.1; -; Genomic_DNA.
DR   PIR; G83775; G83775.
DR   RefSeq; WP_010897177.1; NC_002570.2.
DR   AlphaFoldDB; Q9KE51; -.
DR   SMR; Q9KE51; -.
DR   STRING; 272558.10173622; -.
DR   PRIDE; Q9KE51; -.
DR   EnsemblBacteria; BAB04726; BAB04726; BAB04726.
DR   KEGG; bha:BH1007; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001258; 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; PF00183; HSP90; 2.
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..625
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062967"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..551
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          552..625
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   625 AA;  72343 MW;  FE784C96267DDBCF CRC64;
     MERKEFKAES KRLLEMMVNS IYSQKEIFLR ELISNASDAI DKIYYRALSD DSITFNKDDY
     FIKVTANKED RTLTVSDTGI GMTKEELESN LGTIAKSGSL AFKTENESKD GHDIIGQFGV
     GFYSAFMVAD KVTVTTKALG EESGYQWEST GADGYTILPI AKESVGTEIR LKLKENSEDE
     SYDEFLEEYR LTSIIKKYSD FIRYPIKMDV TKRELKEGTE DEYEDVIEEQ TINSMVPIWR
     KNKNELKDED YTNFYHEKRY GFDQPLKHIH ISVDGAVRYN AILFIPENIP FDYYTKEFEK
     GLELYSNGVL IMEKCPDLLP DYYSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNIKNK
     ITSHLKTLLK DEREKFEQFY RSFGRQLKYG VYSDFGANKE DLQDLLLFYS STEKKMVTLD
     EYVSRMKEDQ PYIYYATGES YARIEKLPQT EMVADKGYEI LYFTEDVDEF AIKMLASYKE
     KEFRSVSSGD LGFEDDEQKD TAADTDEQKE LFEHMKTILD GKVKDVRASK RLKSHPVCLT
     AEGEVSIEME KVLRAMPDNQ NVQAEKVLEI NVNHDVFDVL KASFESDKDK VDLYTKLLYN
     QALLIEGLPV EDPVAFSNDI CKVMA