ID   HTPG_SHESH              Reviewed;         638 AA.
AC   A8FX83;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Ssed_2849;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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; CP000821; ABV37456.1; -; Genomic_DNA.
DR   RefSeq; WP_012143186.1; NC_009831.1.
DR   AlphaFoldDB; A8FX83; -.
DR   SMR; A8FX83; -.
DR   STRING; 425104.Ssed_2849; -.
DR   EnsemblBacteria; ABV37456; ABV37456; Ssed_2849.
DR   KEGG; sse:Ssed_2849; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002015; 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; Stress response.
FT   CHAIN           1..638
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081529"
FT   REGION          1..346
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          347..563
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          564..638
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   638 AA;  71788 MW;  62483406820B67B9 CRC64;
     MSQQETHGFQ TEVKQLLNLM IHSLYSNKEI FLRELVSNAA DASDKLRYEA LTNDALYEGD
     GELRVRISTN KEKGTVTIED NGIGMTRDTV IEHLGTIAKS GTADFFKNLS GDESKDSQLI
     GQFGVGFYSS FIVADKVTVR TRAAGHGSDE GVQWESAGEG DFTVDTIVKE TRGTEIVLHL
     REEEKEFADD YRLRSIITKY SDHISVPVEM WEEGTPAIEA TEEQEAVAAT DGQWQSMNKA
     TALWTRNKSD VSKEEYEEFY KHISHDFTDP LLWSHNRVEG KQEYTSLLYI PSKAPWDMWN
     RDRKHGLKLF VQRVFVMDDA EQFMPSYLRF VQGLIDSNDL PLNVSREILQ DNKVTTALRT
     AVTKRVLGML EKLAKNDAEK YQTFWAEFGQ VLKEGPAEDM VNKERIAGLL RFASTHTEDA
     APTVSLADYV SRMQEGQSKI YYIVADSHEA AANSPHLELL RKKGIEVVLM SERIDEWLIN
     HLTDFDGKQL HSVTRGDLEL GDLEDAGEKE AQEKLETESE GLVKRIKDSL GEKVSAVKVT
     TRLTDTPACV VAGEGEMSTQ MIKLMEAAGQ AVPESKPTFE INPEHPLVAR LNDEQDEALF
     AQWSDLLLQQ AQLSEKGSLA DPSAFIKLMN EMLLAKLK