ID   HTPG_RICCN              Reviewed;         621 AA.
AC   P58478;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=RC1302;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03840.1; -; Genomic_DNA.
DR   PIR; F97862; F97862.
DR   RefSeq; WP_010977860.1; NC_003103.1.
DR   AlphaFoldDB; P58478; -.
DR   SMR; P58478; -.
DR   EnsemblBacteria; AAL03840; AAL03840; RC1302.
DR   KEGG; rco:RC1302; -.
DR   PATRIC; fig|272944.4.peg.1494; -.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000816; 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; 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..621
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063010"
FT   REGION          1..328
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          329..544
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          475..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..621
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   COMPBIAS        481..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  70804 MW;  FF6E5B352DD8F017 CRC64;
     MIQEKKKFDA EVGKILNLMI HSLYSNKEIF MRELISNASD ACDKLRYLSQ SNSELVAGDS
     NFKITVKVDK DHRQIIIRDN GIGMNKDDLI ENLGTIARSG TANFLKSLSG DSKKDNMLIG
     QFGVGFYSSF MVADKVTVTS RKAGEDKVHI WESDGLGEYT VSDSDKEFTR GTEIVLHIKK
     EEDTFLDHFR LKHIVKSYSD HIAVPIYFFD EAGNNEIQLN SASALWTRPK SEITEEQYKE
     FYKSLSYAID DPWITMHNKN EGAIEFTNLL FIPSSKTFDL FHPDRKRRVK LYIKRVFISD
     ENIDLIPSYL RFLRGVVDSE DLPLNISRES LQHNSVLEKI KNAITKRVLG ELRKKKEESP
     EEYNKFWANF GGALKEGLCE ATTNHEKLLE VCIFRSALHN KMISLDEYIA NFKEGQSTIY
     YLSGDNPDKL LSSPQIEGLL SKKIDVLLFT DTVDDFWVNV NSKYKEHAIK SATRSDIDVE
     QTTSQSEEKN TDSTKSNDEY KLLTDYFKET LGELVKEVKI SKKLTSSPAC LAVSDAAMDI
     RMERFLIEQK QIANASAKNL ELNPKNKIIE KIFNDLKANN KNNEELVNLI FDQACILEGE
     PVADTGAFSK RLNDIVQKAI L