ID   HTPG_GEOMG              Reviewed;         650 AA.
AC   Q39SQ3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Gmet_2498;
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) 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; CP000148; ABB32721.1; -; Genomic_DNA.
DR   RefSeq; WP_004514648.1; NC_007517.1.
DR   AlphaFoldDB; Q39SQ3; -.
DR   SMR; Q39SQ3; -.
DR   STRING; 269799.Gmet_2498; -.
DR   PRIDE; Q39SQ3; -.
DR   EnsemblBacteria; ABB32721; ABB32721; Gmet_2498.
DR   KEGG; gme:Gmet_2498; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000007073; 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..650
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236995"
FT   REGION          1..349
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          350..566
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          567..650
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   650 AA;  74043 MW;  083ECD4AD97C6D40 CRC64;
     MTKTTKKFET EVQQLLDLVI HSLYSNKDIF LRELISNSSD AIDKVLFEAH QNAAVIEGEP
     EGKIKLIPDK EAGTITIRDN GVGMTMEEVE KNIGTIAHSG TKAFLANLKE QNVSEHPELI
     GQFGVGFYAS FMVADRVTLV TRRAGQDKAA GVRWESTGDG TYTVEEAVKE TRGTEITLHL
     KEEMKEYLDE WKIRSIVRKY SDYVQYPVVM DVTRTEVPKG VNGEEIEGAG TIEKTVEETL
     NSMKAIWARA KSEVTEEEYE EFYKHVSHDF EKPLKTIHYS AEGVSEFKAL LYLPAHKPFD
     LFMPERKKGV QLYVRRVFIT DSCEQLIPDY LRFVKGVVDS SDLPLNVSRE ILQEDVQIKR
     IQKSLVSKII STLSEMREKE ADDYLAFYKE FGQVLKEGVH FDYANREKLQ DLLLFESTRT
     EAGKFTSLKE YVERMPAGQE EIYFITGTSR TALEQSPHLE IFRKKEYEVL FLTDPVDEWV
     VQGVTEYDGK KLKAVDRGDV IPATEEEKKE QEAKREEAFK QYGDLLSFVK EKLDARVKEV
     RLSSRLTDSA CCLVADEHGL NANMERILRA MNQDVPESKR ILELNPDHPL MQVMANLFAR
     DKANPRLGDY CDLLYDQALL TEGSPISDPL RFTRLVAELM VADGKAAAGE