ID   HTPG_RHOJR              Reviewed;         642 AA.
AC   Q0S467;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 101.
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};
GN   OrderedLocusNames=RHA1_ro05892;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG97669.1; -; Genomic_DNA.
DR   RefSeq; WP_011597982.1; NC_008268.1.
DR   AlphaFoldDB; Q0S467; -.
DR   SMR; Q0S467; -.
DR   STRING; 101510.RHA1_ro05892; -.
DR   EnsemblBacteria; ABG97669; ABG97669; RHA1_ro05892.
DR   KEGG; rha:RHA1_ro05892; -.
DR   PATRIC; fig|101510.16.peg.5935; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000008710; 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; 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; 2.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..642
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258521"
FT   REGION          1..348
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          349..564
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          565..642
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   642 AA;  72562 MW;  000D6F5AB6EAD0C1 CRC64;
     MSTKIEQLEF QAETRQLLDL MIHSVYSNKD SFLRELISNA SDALDKLRLE AFRNKELHVD
     TSDLHVEIEV DAEKRTLTVR DNGIGMSHDE VVDLIGTLAK SGTADLRRKL KEAKDAAASE
     ELIGQFGIGF YSTFMVADKV TLLTRKAGES EATRWESSGE ATYTIEAVDD APQGSSVTLH
     LKPEDAEDHL HDYTSERKIK ELVKRYSDFI AWPIRMNVER TVPAEGDGED EVTTTSETIN
     SMKALWARSK DDVSEDEYKE FYKHIAHAWD DPLEVIPMKA EGTFEFQALL FIPSHAPFDL
     FMRDGKTGVQ LYVKRVFIMD DCDQLMPEYL RFVKGVVDAQ DLSLNVSREI LQQDRQIRAI
     RRRLTKKVLT TIKDLKTERP DDYRTFWAEF GRAVKEGLMS DTDNRDVLLG ISSFASTHSE
     EELTSLEDYV ARMKDGQEQI FYATGESRQL LESSPHMEAF RAKGFEVLLL TDPVDEMWVG
     AVPEFDGKSF QSIAKGEVDL DTEEDKKAHE SEREEQEKDF AGLLSWMADA LSEQVKEVRL
     STRLTTSPAC IVGDAFSMSP ALERMYRASG QPVPVTKRIL ELNPTHPLVT GLREAHGERN
     EDPALGETAE LLYGMALLAE GGELEDPARF TTMLANRLAR TV