ID   HTPG_SHEHH              Reviewed;         639 AA.
AC   B0TP05;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Shal_1596;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000931; ABZ76162.1; -; Genomic_DNA.
DR   RefSeq; WP_012276700.1; NC_010334.1.
DR   AlphaFoldDB; B0TP05; -.
DR   SMR; B0TP05; -.
DR   STRING; 458817.Shal_1596; -.
DR   PRIDE; B0TP05; -.
DR   EnsemblBacteria; ABZ76162; ABZ76162; Shal_1596.
DR   KEGG; shl:Shal_1596; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001317; 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..639
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081527"
FT   REGION          1..347
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          348..564
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          565..639
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   639 AA;  71935 MW;  B3A9EE7581AF09D6 CRC64;
     MSQQETHGFQ TEVKQLLHLM IHSLYSNKEI FLRELVSNAA DAADKLRYEA LTNDALYEGD
     GELRVRISAD KEKGTVTIED NGIGMTRDGV IEHLGTIAKS GTAEFFKNMS GDESKDSQLI
     GQFGVGFYSS FIVADRVTVR TRAAGHSADE AVLWESAGEG DFTVETITKQ SRGTEITLHL
     RDDEKEFADD YRLRSIITKY SDHISVPVEM YEEGTPAVEA TEEGGEAIPA TEGHWKLMNK
     ATALWTRNKS DVSDEEYQEF YKYISHDFTD PLLWSHNRVE GKQEYTSLLY IPAKAPWDMW
     NRDRKHGLKL FVQRVFVMDD AEQFMPSYLR FVQGLIDSND LPLNVSREIL QDNKVTTALR
     TAVTKRVLGM LEKLAKNDAE KYQSFWTEFG QVLKEGPAED FANKERVAGL LRFASTHTGE
     ATANVSLADY VERMKEGQSK IYFIVADSYE AAANSPHLEL LRKKGIEVLL MSERIDEWLI
     NHLTEFDGKK LHSVTRGDLE LGELEDASEK EAQEKLETES EGLVKRVKDS LGDKVSAVKV
     TTRLTDTPAC VVAGEGEMST QMIKLMQAAG QDVPESKPTF ELNPEHPLVA RLNDEQDEQR
     FAQWSELLLQ QALLSEKGSL ADPSAFIKLM NQMLLASVK