ID   HTPG_CUPMC              Reviewed;         633 AA.
AC   Q1LKE3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Rmet_2506;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(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; CP000352; ABF09383.1; -; Genomic_DNA.
DR   RefSeq; WP_008648084.1; NC_007973.1.
DR   AlphaFoldDB; Q1LKE3; -.
DR   SMR; Q1LKE3; -.
DR   STRING; 266264.Rmet_2506; -.
DR   PRIDE; Q1LKE3; -.
DR   EnsemblBacteria; ABF09383; ABF09383; Rmet_2506.
DR   KEGG; rme:Rmet_2506; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002429; 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; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..633
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258519"
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;  71067 MW;  63CAC5B488AADA62 CRC64;
     MTAPHETMSF QAEVKQLLHL MIHSLYSNKE IFLRELVSNA SDATDKLRFE AIANPALLEN
     DADLAIRIEA DPAARTLKIT DNGIGMSRDE AIRNLGTIAR SGTKEFFQQL SGDQQKDAAL
     IGQFGVGFYS AFIVADKVTV ETRRAGLAAD EAVRWESAGD GEFSIDAINR AERGSTITLH
     LREGEDDFLS SYRLQNIIRK YSDHISLPIR MPKEEWDAEA QQQKVTGEWE SVNQASALWT
     RSKSDITDEQ YQAFYQHIAH DHEAPLAWTH NRVEGRSEYT QLLYIPARAP FDLWDRNHKA
     GLKLYVKRVF IMDDADQLLP AYLRWVKGVV DSADLPLNVS RELLQESRDV KAIREGCAKR
     VLSMLEAMAD SEDEAERAKY KTFWEQFGQV LKEGVGEDHG NGERIAKLLR FATTHGDTAE
     QSVSLVDYVG RMKEGQDKIY YVTADTWVAA KSSPHLEVFR KKGIEVVLLT DRVDEWLLSY
     LHEFDGKQLV SVARGDLDLG ALADEAEKAE QEKASADWKE VVDRAKSVLE GKAKDVRVTL
     RLTDSASCLV SDDGDMSGYL QRLLKQAGQK APDAQPILEL NPEHALVKKL RDLPDGEAFG
     DRVRVLFDQA LLAEGGMLDD PAAYVQRVNR LLA