ID   HTPG_ALKCK              Reviewed;         625 AA.
AC   Q5WJE6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, 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=ABC0970;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD63509.1; -; Genomic_DNA.
DR   RefSeq; WP_011245825.1; NC_006582.1.
DR   AlphaFoldDB; Q5WJE6; -.
DR   SMR; Q5WJE6; -.
DR   STRING; 66692.ABC0970; -.
DR   PRIDE; Q5WJE6; -.
DR   EnsemblBacteria; BAD63509; BAD63509; ABC0970.
DR   KEGG; bcl:ABC0970; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001168; 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; 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   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_0000224196"
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;  72747 MW;  6E3D25B8EFE3F8EA CRC64;
     MEKKQFQAES KRLLEMMVNS IYSQKEIFLR ELISNASDAI DKMYYRSLTD DSLSFEKDRY
     AIYVEADKDN RKLVMKDTGI GMTKEELEAN LGTIAKSGSL AFKKETEIED GHDIIGQFGV
     GFYAAFMVAD KVTVITRSID SDQAYKWESD GTDGYTIEPA EKEDVGTVIT LHIKENTDDE
     SYDEYLEEYR IKAIIKKYSD FIRYPIKMNV TVSKPKEDNE DEYAEYQEEQ TINSMVPIWR
     KNKSELKDSD YEQFYQDKRY GFDKPLEHIH VSVDGAIRYN AILFIPEHTP FDYYSKEYEK
     GLELYANGVL IMEKCAELLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNIKSK
     IKSQLKTMLK KEPDKYEKFY KAFGRQLKFG VYNDFGANKD DLQDLLLFYS STEKKLVSLS
     DYVSRMKEGQ TYIYYATGES NERIAKLPQT EMVADQGYEI LYFTEDVDEF AIKMLRSYDE
     KEFMSVSSAD LDIETDEKQE EETNSEENKK LFEKMKSILD GKVKDVRTSK RLKSHPVFLA
     ADGEITLEME KVLQAMPDNQ NVKAEKVLEI NPNHDVFHSL KQAYEEDEDK LKLYTNLLYN
     QALLIEGLPL EDPVEFSQNM CKVMV