ID   HTPG_SHEPA              Reviewed;         638 AA.
AC   A8H2R4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Spea_1526;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
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.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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; CP000851; ABV86851.1; -; Genomic_DNA.
DR   RefSeq; WP_012154775.1; NC_009901.1.
DR   AlphaFoldDB; A8H2R4; -.
DR   SMR; A8H2R4; -.
DR   STRING; 398579.Spea_1526; -.
DR   EnsemblBacteria; ABV86851; ABV86851; Spea_1526.
DR   KEGG; spl:Spea_1526; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002608; 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..638
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081528"
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;  71882 MW;  219E0037A251B304 CRC64;
     MSQQETHGFQ TEVKQLLHLM IHSLYSNKEI FLRELVSNAA DAADKLRYEA LTNDNLYEGD
     GELRVRISAD KEKGTVTIED NGIGMTRDGV IEHLGTIAKS GTADFFKKLS GDESKDSQLI
     GQFGVGFYSS FIVADRVTVR TRAAGHSADE AVLWESAGEG DFTVETISKQ TRGTEITLHL
     RDDEKEFADD YRLRSIITKY SDHISVPVEM FEAGTPAVEA TEDTEAVAAT EGSWKPMNKA
     TALWTRNKSD VSDEEYQEFY KHISHDFTDP LLWSHNRVEG KQEYTSLLYI PAKAPWDMWN
     RDRKHGLKLF VQRVFVMDDA EQFMPSYLRF VQGLIDSNDL PLNVSREILQ DNKVTTALRT
     AVTKRVLGML EKLAKNDAEK YQSFWTEFGQ VLKEGPAEDF ANKERIAGLL RFASTHTGEA
     TPNVSLADYI ERMQEGQSKI YYIVADSHEA AANSPHLELL RKKGIEVLLM SERIDEWLIN
     HLTEFDGKKL HSVTRGDLEL GELEDDDEKE AQEKLQTESE GLVKRVKDSL GDKVSEVKVT
     TRLTDTPACV VAGEGEMSTQ MIKLMQAAGQ DVPEPKPTFE LNPEHPLVAR LNDEQDEQQF
     AQWSELLLQQ ALLSEKGSLA DPSAFIKLMN QMLLASVK