ID   HTPG_ALBFT              Reviewed;         663 AA.
AC   Q21SJ8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Rfer_3551;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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; CP000267; ABD71255.1; -; Genomic_DNA.
DR   RefSeq; WP_011465818.1; NC_007908.1.
DR   AlphaFoldDB; Q21SJ8; -.
DR   SMR; Q21SJ8; -.
DR   STRING; 338969.Rfer_3551; -.
DR   PRIDE; Q21SJ8; -.
DR   EnsemblBacteria; ABD71255; ABD71255; Rfer_3551.
DR   KEGG; rfr:Rfer_3551; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008332; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..663
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258522"
FT   REGION          1..352
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          218..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..595
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          596..663
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   663 AA;  72925 MW;  FA989F0A81476651 CRC64;
     MTKQTLSFQA EVAQLLHLVT HSLYSNKEIF LRELISNASD ACDKLRYEAI NDSGLYEDAP
     TLEVRVSFDP AAKTLTISDN GIGMSAQEAI DHLGTIAKSG TKDFVSKLSG DQKADSQLIG
     QFGVGFYSGF IVADKITVES RRAGMKASEG VRWISGGAGD FEVETIERAA RGTSVILHLR
     DDAMDYCSAW KLKSIINKYS DHISLPILME KEEWKDGELI NPSDEKGGRQ PGGMVKTGEW
     ETVNKGNAIW ARAKKDITPE QYTEFYKQIS HDFEAPLAYT HNRVEGSTEY TQLLYLPSKA
     PMDLFNREKS AGVKLYVKRV FIMDDAEALL PTYLRFVKGV VDSADLPLNV SRELLQESRD
     VKAIREGCTK RVLGMLEDLA KHDKLPAPSA DGGTDTTAGV SDVLSEEDKA NEGKYSKFYA
     EFGAVLKEGL GEDYANKDRL AKLLRFASSS TDTVSVSFAD YKARMKEGQE AIYYITADTP
     AAAKNSPQLE VFKKKGIEVL LMTDRVDEWA LNYLQEFDGT PLQSVAKGAV DLGKLQDEAE
     KKAAEEAAET FKPLLAKLKE ALKDKAEDVR VTTRLVDSPA CLVVQDHGMS TQLARMLKQA
     GQAAPDVKPV LEVNAEHPLV KKLDGSVHFN DLAHILFDQA LLAEGGLPAD PAAYVKRVNA
     LLV