ID   HTPG_RALSO              Reviewed;         640 AA.
AC   Q8Y0Q3;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=RSc0990;
GN   ORFNames=RS04302;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(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; AL646052; CAD14692.1; -; Genomic_DNA.
DR   RefSeq; WP_011000942.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y0Q3; -.
DR   SMR; Q8Y0Q3; -.
DR   STRING; 267608.RSc0990; -.
DR   EnsemblBacteria; CAD14692; CAD14692; RSc0990.
DR   GeneID; 60500498; -.
DR   KEGG; rso:RSc0990; -.
DR   PATRIC; fig|267608.8.peg.1006; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001436; 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..640
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063006"
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..640
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   640 AA;  71408 MW;  2E5F7F0D48D07B8C CRC64;
     MGAPHEKMAF QAEVKQLLHL MIHSLYSNKE IFLRELVSNA SDAVDKLRFE GIADPSLLEG
     GGELGIRIGF DAQARTVTIA DNGIGMSRDE AIRNLGTIAR SGTREFFSQL SGDQQKDAAL
     IGQFGVGFYS AFIVADRVTV ESRRAGVPAA EGVRWESAGD GEFTVDAIER AERGTTITLH
     LREGEDDFLS AWRLKSIVQK YSDHISLPIA MRKESWDEEK KEMVAQDEWE TINQASALWA
     RPRADVTDEQ YIAFYQHIAH EQGQPLAWTH NRVEGRSEYT QLLYLPTNAP FDLWDRERRS
     GLKLYVKRVF IMDDAEQLLP AYLRFVKGVI DSADLPLNVS REILQESRDV KAIREGSTKR
     VLGMLESMAD SDDAAEKDKY ATFWQHFGQV LKEGLGEDFA NKDRIAKLLR FASTHNAGDE
     QTVSLADYIG RMKDGQDKIY YVSAENWTAA KSGPHLEVFR KKGVEVLLLT DRVDEWMLSF
     LHDFEEKALV SVARGGLDLG ALEDEAERAE HAKVEGEFKP LVDRAKAVLA DKAKDVRITH
     RLTDSPSCLV ADEGDISGTL ARLLKQAGQK APDTKPVLEL NPAHPLVRKL ALLESVTGGE
     ADRAAFEDRL HVLFDQALLA EGGSLADPAD YVQRVNRLLA