ID   HTPG_RICPR              Reviewed;         621 AA.
AC   Q9ZCB9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, 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=RP840;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235273; CAA15264.1; -; Genomic_DNA.
DR   PIR; H71645; H71645.
DR   RefSeq; NP_221188.1; NC_000963.1.
DR   RefSeq; WP_004599674.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCB9; -.
DR   SMR; Q9ZCB9; -.
DR   STRING; 272947.RP840; -.
DR   EnsemblBacteria; CAA15264; CAA15264; CAA15264.
DR   GeneID; 57569963; -.
DR   KEGG; rpr:RP840; -.
DR   PATRIC; fig|272947.5.peg.878; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002480; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..621
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063011"
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          545..621
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   621 AA;  70713 MW;  9F97B97801524007 CRC64;
     MTQEKKKFDA EVGKILNLMI HSLYSNKEIF MRELISNASD ACDKLRYLSQ SNSELIAGDS
     NFKIIVKVDK DNGQIIIRDN GIGMNKEDLI ENLGTIARSG TANFLKNLSG DSKKDNMLIG
     QFGVGFYSSF MVADKVTVTS RKAGESKVHT WESDGLGEYI VADSEQEFTR GTEIVLYIKK
     SETTFLDHFR LKHIVKSYSD HIAVPIYFCD EAGNNEIQLN SASALWTRPK SEITEDQYKE
     FYKSLSYAVD DPWVTLHNKN EGAIEFTNLL FIPSSKTFDL FHPDRKKRVK LYIKRVFISD
     ENIDLIPSYL RFLRGVVDSE DLPLNISRES LQHNNVLEKI KNAITKRVLG ELRKKKEELP
     EEYNKFWTNF GGALKEGLCE ATTDHEKLLE VCIFRSALHN KMISIDEYIA NFKEGQNTIY
     YLSGDNPDKL LSSPQIEGLL NKNIDVLLFT DTVDDFWVNV NSEYKGYAIK SATRSDIDVE
     QTTSQPKDKN TDSKKSDNEY KLLTDYFKEI LGELVKEVKI SKKLTLSPAC LAVSDTAMDI
     RMERFLIEQK QIANASAKNL ELNPKNKIIE KIFNDLKANN KNNNELVNLI FDQACILEGE
     PVADTGAFSK RLNDILQKAI L