ID   HTPG_OLEA2              Reviewed;         636 AA.
AC   Q313E8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Dde_1147;
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB37948.1; -; Genomic_DNA.
DR   RefSeq; WP_011367169.1; NC_007519.1.
DR   AlphaFoldDB; Q313E8; -.
DR   SMR; Q313E8; -.
DR   STRING; 207559.Dde_1147; -.
DR   PRIDE; Q313E8; -.
DR   EnsemblBacteria; ABB37948; ABB37948; Dde_1147.
DR   KEGG; dde:Dde_1147; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002710; 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; 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   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..636
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236991"
FT   REGION          1..329
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          330..550
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          551..636
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   636 AA;  72196 MW;  E16A7F968637A610 CRC64;
     MSKEHGAAAE KHEFRTEVRK LLHIITHSLY TNREIFLREL VSNASDALDK LRFAQTRGEA
     APAADLDLNI AITVNEETRT LTVSDTGIGM TRQELIDNLG TIASSGSERF LKELAEKGEQ
     ASNIIGRFGV GFYAVFMVAD SVTVTTRSAL DASGAWRWTS DGLGSFELEE ALDAPERGTR
     IDIRLKEDAG DFLKKDHLKD VIRRHSNFIP FPVSVEGEHV NTTPALWREP RFQVTEEQYK
     DFYTFLTFDT QAPMDTIHLS IDAPVQFTSL AFIPNFGNEL FGYDRDKYGL DLYVRRVLIS
     KEYKALIPEY LSFLKGVVDT EDLPLNISRE TLQENALIAK IRQTLVKQVL AHLAKLAESD
     AEKYATFWRT HGRVFRMGYN DYINRDKFIP LLRFNSSALD DEKGLCSLDD YIGRAREGQK
     TVWYVSAPNR EAARLNPHVE IFRRKGIEVL YLYEAADEFI MESLGKWNEF EFRSAEHADA
     DALKDFDDVE KKDAPEALDE EGRKTLSSLL SHMKTLLGDK VEDVRESARL SDSPACLASK
     DGGMTASMEK LMRVMNKDES VPRKVLEINP DHPLTRNLLR LYRADADDRL LAQATEQLYE
     SALLLEGYLR DPHALVGRVN SLLEQATGWY AEVRKL