ID   HTPG_SHESW              Reviewed;         637 AA.
AC   A1RIQ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-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};
GN   OrderedLocusNames=Sputw3181_1709;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-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; CP000503; ABM24546.1; -; Genomic_DNA.
DR   RefSeq; WP_011789043.1; NC_008750.1.
DR   AlphaFoldDB; A1RIQ1; -.
DR   SMR; A1RIQ1; -.
DR   KEGG; shw:Sputw3181_1709; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002597; 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..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014960"
FT   REGION          1..345
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          346..562
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          563..637
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   637 AA;  71943 MW;  08458A7DC19506B8 CRC64;
     MSQQETHGFQ TEVKQLLHLM IHSLYSNKEI FLRELVSNAA DAADKLRYLA LTNDALYEGD
     GELRVRISAD KDKGTVTIED NGVGMTRDGV IEHLGTIAKS GTAEFFKNLS GEASKDSQLI
     GQFGVGFYSA FIVAKKVTVR TRAAGHKADE AVLWESEGEG SFTVETITKA SRGTEITLHL
     RDEEKEFADD WRLRSIITKY SDHISVPVEM WQEGTPERDG PDGEKIPATE GYWKVMNKAT
     ALWMRNKSEI SDEEYQEFYK HISHDYTDAL LWSHNRVEGK QEYTNLLYIP SKAPWDLWNR
     DRKHGLKLFV QRVFIMDDAE QFMPSYLRFV QGLIDSNDLP LNVSREILQD NHITKAMRTG
     ITKRVLGMLE KLAKDDAEKY QQFWAEFGQV LKEGPAEDFA NRERIAGLLR FASTHTGSAA
     PTVSLDDYIS RMKEGQTKIY YIVADSYDAA ANSPHLELLR KKDIEVLLMS ERIDEWLINH
     LTEYKEKQLH SVTRGELELG ELEDAAEKEA QEKLAEESAP LIERIKAALG TKVADVKVTS
     RLTDTPACVV TGEGEMSTQM IKLMQAAGQP VPEVKPTFEV NPAHPLVSRL NDLQDETAFA
     DWSNLLLQQA QLSEKGSLAD PSAFIKLMNQ MLLANMK