ID   HTPG_GEOUR              Reviewed;         645 AA.
AC   A5GER7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Gura_1728;
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-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; CP000698; ABQ25922.1; -; Genomic_DNA.
DR   RefSeq; WP_011938628.1; NC_009483.1.
DR   AlphaFoldDB; A5GER7; -.
DR   SMR; A5GER7; -.
DR   STRING; 351605.Gura_1728; -.
DR   PRIDE; A5GER7; -.
DR   EnsemblBacteria; ABQ25922; ABQ25922; Gura_1728.
DR   KEGG; gur:Gura_1728; -.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000006695; 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   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..645
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081517"
FT   REGION          1..348
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          349..565
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          566..645
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   645 AA;  73915 MW;  94C3D838F534C4FB CRC64;
     MTKSTKKFET EVQQLLDLVI HSLYSNKDIF LRELVSNASD AIDKVKFESH SNMDILEGNT
     DWKIKLIPDK TAGTLTIRDN GIGMNVVEVE ENIGTIARSG TRAFMENLKD KNVQNNPELI
     GQFGVGFYAS FMVADKVTLI TRKAGDKNAA CRWESTGDGS YTIEDCEKET RGTDITLHLK
     DEMKEYLDEW KIRSIIKKYS DYVQYPVVMD VTRDEPAKGV DGEVIEGGGT IEKTTEETLN
     SMKAIWTRAK SEISEEEYEE FYKHISHDYD KPFRTIHYSA EGTSEFKALI YIPSHKPFDL
     FMRDHKKGVH LYVKRVFITD NCEALLPDYL RFMKGVVDSS DLPLNVSREI LQEDIQIKRI
     EKNLVGKILS TLVETKEKTP EDYLKFYKEF GPVLKEGVHF DHANKEKLQE LILFESSKTE
     AGNYISLKEY VARMPEAQKE IYYITGASRS ALENSPHLEI FRKKGFEVLY MTDPVDEWVV
     QSLTDYDGKK LHAVDRGDLE LDSAEEKKEK EAKQEEAKKQ YQGVLDFVKE QLKDKVKEVR
     FSSRLTDSAC CLVADEYGLN ANMEKILKAM NQDVPESKRV LELNPDHPLM QVLSSIFEKD
     KENPRLADYC GLLYDQALLT EGSPVPDPLR FTRLVAELMV KAAEK