ID   HTPG_CUPTR              Reviewed;         633 AA.
AC   B3R5J8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=RALTA_A2146;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ70083.1; -; Genomic_DNA.
DR   RefSeq; WP_012353388.1; NC_010528.1.
DR   AlphaFoldDB; B3R5J8; -.
DR   SMR; B3R5J8; -.
DR   STRING; 977880.RALTA_A2146; -.
DR   EnsemblBacteria; CAQ70083; CAQ70083; RALTA_A2146.
DR   GeneID; 29762983; -.
DR   KEGG; cti:RALTA_A2146; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; CTAI977880:RALTA_RS10415-MON; -.
DR   Proteomes; UP000001692; Chromosome 1.
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_1000127027"
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;  71231 MW;  28539DF8F67BF5F3 CRC64;
     MTAPHETMSF QAEVKQLLHL MIHSLYSNKE IFLRELVSNA SDATDKLRFE AIANPSLLEN
     DADLAIRIEA DAKARTLKIT DNGIGMSRDE AIRNLGTIAR SGTKEFFQQL SGDQQKDAAL
     IGQFGVGFYS AFIVADKVTV ETRRAGLGAE EAVRWESTGD GEFTVDAIAR AERGTTITLH
     LREGEDDFLS AWRLKSIIQK YSDHISLPIR MPKEVWDAEA STYKRTDEWE SVNQASALWT
     RAKSDITDEQ YTAFYQHIAH DNEAPLAWTH NRVEGRSEYT QLLYIPARAP FDLWDRNHKA
     GLKLYVKRVF IMDDAEQLLP GYLRWVKGVV DSADLPLNVS RELLQESRDV KAIREGCTKR
     VLSMLETLAD SEDEAERAKY ATFWQQFGQA LKEGVGEDQA NQERVAKLLR FASTHNDTAE
     QNVALAAYVG RMKEGQDKIY YVTADTWSAA KNSPHLEVFR KKGIEVLLLT DRVDEWMLSY
     LREFDGKELV SVARGDLDLG KLADEAEKAE QEKAEADWKD VIERARAVLA GKAKDVRVTL
     RLTESASCLV SDEGDMSGYL QRLLKQAGQK APDAQPILEL NPEHALVKKL RDLPEGEAFS
     DRLQVLFDQA LLAEGGMLED PAAYVQRVNK LLA