ID   HTPG_RICM5              Reviewed;         623 AA.
AC   A8F2Y0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=RMA_1325;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria: evidence
RT   from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
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; CP000683; ABV85266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8F2Y0; -.
DR   SMR; A8F2Y0; -.
DR   EnsemblBacteria; ABV85266; ABV85266; RMA_1325.
DR   KEGG; rms:RMA_1325; -.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001311; 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..623
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127034"
FT   REGION          1..330
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          331..546
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          477..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..623
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   COMPBIAS        483..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  70930 MW;  AE73C99FB2AFAC6D CRC64;
     MIMTQEKKKF DAEVGKILNL MIHSLYSNKE IFMRELISNA SDACDKLRYL SQSNSELVAG
     DSNFKITVKV DKDNGQIIIR DNGIGMNKDD LIENLGTIAR SGTANFLKSL SGDSKKDNML
     IGQFGVGFYS SFMVADKVTV TSRKAGEDKV HIWESDGLGE YTVSDSDKEF TRGTEIVLHI
     KKEEDTFLDH FRLKHIVKSY SDHIAVPIYF FDEAGNNEIQ LNSASALWTR PKSEITEEQY
     KEFYKSLSYA VDDPWITMHN KNEGAIEFTN LLFIPSSKTF DLFHPDRKRR VKLYIKRVFI
     SDENIDLIPS YLRFLRGVVD SEDLPLNISR ESLQHNSVLE KIKNAITKRV LGELRKKKEE
     SPEEYNKFWA NFGGALKEGL CEATTDHEKL LEVCIFRSAL HNKMISLDEY IANFKEGQST
     IYYLSGDNPD KLLSSPQIEG LLSKEIDVLL FTDTVDDFWV NVNSKYKEHA IKSATRSDID
     VEQTTSQSEE KNTDSKKSDD EYKLLTDYFK ETLGELVKEV KISKKLTSSP ACLAVSDAAM
     DIRMERFLIE QKQIANASAK NLELNPKNKI IEKIFNDLKA NNKNNEELVN LIFDQACILE
     GEPVADTGAF SKRLNDIVQK AIL