ID   HTPG_CUPPJ              Reviewed;         633 AA.
AC   Q46YS9;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=Reut_A2342;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ61704.1; -; Genomic_DNA.
DR   RefSeq; WP_011298493.1; NC_007347.1.
DR   AlphaFoldDB; Q46YS9; -.
DR   SMR; Q46YS9; -.
DR   STRING; 264198.Reut_A2342; -.
DR   EnsemblBacteria; AAZ61704; AAZ61704; Reut_A2342.
DR   KEGG; reu:Reut_A2342; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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_0000224226"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..562
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          563..633
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   633 AA;  71266 MW;  2E1858FF4B7DA8A5 CRC64;
     MSAPHETMSF QAEVKQLLHL MIHSLYSNKE IFLRELVSNA SDATDKLRFE AIANPSLLEN
     DADLAIRIEA DTAARTLKIT DNGIGMSRDE AIRNLGTIAR SGTKEFFQQL SGDQQKDAAL
     IGQFGVGFYS AFIVADKVTV ETRRAGVAAD EAVRWESTGD GEFTVDAITR AERGTTITLH
     MREGEDDFLS AWRLKSIIQK YSDHISLPIR MPKEVWDADT SAYKRTDEWE SVNQASALWT
     RPKSDITDEQ YIAFYQHIAH DNEAPLSWTH NRVEGRSEYT QLLYIPARAP FDLWDRNHKH
     GLKLYVKRVF IMDDAEQLLP SYLRWVKGVI DSADLPLNVS RELLQESRDV KAIREGSTKR
     VLSMLESLAD SEEEAERAKY TTFWQQFGQA LKEGLGEDNA NQERIAKLLR FASTQNDNAE
     QSVSLAAYVG RMKEGQDKIY YVTADTWAAA KNSPHLEVFR KKGIEVLLLT DRVDEWMLSF
     LREFDGKELV SVARGDLDLG SLADEAEKAE QEKAETEWKD VVARAKTVLE GKAKDVRVTL
     RLTASASCLV SDEGDMSGYL QRLLKQAGQK APDAQPILEL NPEHALVKKL RDLPEGDGFN
     DRLLVLFDQA LLAEGGMLDD PAAYVQRVNK LLA