ID   HTPG_OCEIH              Reviewed;         625 AA.
AC   Q8CX68;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=OB3158;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC15114.1; -; Genomic_DNA.
DR   RefSeq; WP_011067555.1; NC_004193.1.
DR   AlphaFoldDB; Q8CX68; -.
DR   SMR; Q8CX68; -.
DR   STRING; 221109.22778846; -.
DR   PRIDE; Q8CX68; -.
DR   EnsemblBacteria; BAC15114; BAC15114; BAC15114.
DR   KEGG; oih:OB3158; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   PhylomeDB; Q8CX68; -.
DR   Proteomes; UP000000822; 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; 1.
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_0000062999"
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;  72319 MW;  EF28E13EA5BCA047 CRC64;
     MGKRKFKAES QKLLDMVINS IYSQREVFLR ELISNASDAI DKIYYKALTD DSLSFDVDNY
     YIKITPNKEE RTLTVVDTGI GMTKEELENN LGVIAKSGSH TFKSENEIKD GHDIIGQFGV
     GFYAAFMVAD KVEVVTKSID SDAAFKWESK GSDGYSITEA DKQDIGTTIT LYIKENQEEE
     NYDEFLDTFT LQQIIKKYSD FIRYPIKMDV TESKLKEGSE DEYEDVVEEQ TINTMVPIWK
     KNKSELTDDD YTNFYQEKRY GFDKPLKHVH INVDGSIRYN AILFIPESAP FNYYTRDYEK
     GLELYSNGVL IMDKCADLLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNIKKK
     VKQQLVSLLR DERENYEKFF DAFGQQIKFG VYSDYGQNKD ELKDLLLFYS SKEKKLVTLE
     EYVSCMPEDQ KYIYYATGDS RDRIEKLPQT ELVADKGYEI LYFTDEIDEF AIKMLMNYDE
     KEFRSVSSGD LGIEEDEKEE NEQENNDNAE LFTAMKEVLS TKVKDVRASK RLKSHPVVLT
     ADGEISLEME KIINAMPDDQ QIQADKVLEI NVNHDIFQSL KAAQGNDDEK FKLYTNLLYN
     QALLIEGLPI NDPVEFTNDI CKVMV