ID   HTPG_RICAH              Reviewed;         621 AA.
AC   A8GQ51;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=A1C_06515;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000847; ABV75526.1; -; Genomic_DNA.
DR   RefSeq; WP_012150155.1; NC_009881.1.
DR   AlphaFoldDB; A8GQ51; -.
DR   SMR; A8GQ51; -.
DR   STRING; 293614.A1C_06515; -.
DR   PRIDE; A8GQ51; -.
DR   EnsemblBacteria; ABV75526; ABV75526; A1C_06515.
DR   KEGG; rak:A1C_06515; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000006830; 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; Stress response.
FT   CHAIN           1..621
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014945"
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..495
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..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  70807 MW;  A28ADD7EA36A374C CRC64;
     MTQEKKKFDA EVGKILNLMI HSLYSNKEIF MRELISNASD ACDKLRYLSQ SHSELVASDS
     NFKITVKVDK DNWQIIIRDN GIGMNKEDLI DNLGTIARSG TANFLKSLSG DSKKDNMLIG
     QFGVGFYSSF MVADKVTVTS RKAGEDTVHV WESDGLGEYI VSDSDKEFTR GTEIILHIKK
     EEDIFLDHFR LKHIVKSYSD HVAVPIYFFD EAGNNEIQLN SASALWTRPK SEITEEQYKE
     FYKSLSYAVD DPWITMHNKN EGAIEFTNLL FIPSSKTFDL FHPDRKRRVK LYIKRVFISD
     ENIDLIPSYL RFLRGVVDSE DLPLNISRES LQHNSVLEKI KNAITKRVLG ELRKKKEESS
     EEYNKFWANF GGALKEGLCE ATTDHEKLLE VCIFRSALHN KMISLDEYIA GFKEEQNTIY
     YLSGDNPDKL LSSPQIEGLL SKNIDVLLFT DTVDDFWVNV NSEYKGHAIK SATRSDIDVE
     QTTSQSEDKN THSKKSDDEY KLLTDYFKET LGKLVKEVKI SKKLTSSPAC LAVSDSAMDI
     RMERFLIEQK QITAASAKNL ELNPKNKIIE KIFNDLKANN KNNEELVNLI FDQACILEGE
     PVADTGAFSK RLNDIVQKAI L