ID   HTPG_SHEAM              Reviewed;         637 AA.
AC   A1S564;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Sama_1313;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
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; CP000507; ABL99520.1; -; Genomic_DNA.
DR   RefSeq; WP_011759429.1; NC_008700.1.
DR   AlphaFoldDB; A1S564; -.
DR   SMR; A1S564; -.
DR   STRING; 326297.Sama_1313; -.
DR   PRIDE; A1S564; -.
DR   EnsemblBacteria; ABL99520; ABL99520; Sama_1313.
DR   KEGG; saz:Sama_1313; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000009175; 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..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014950"
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;  71637 MW;  693FF5ECA7FAFFDF CRC64;
     MSHQETHGFQ TEVKQLLHLM IHSLYSNKEI FLRELVSNAA DAADKLRYLA LTNDSLYEGD
     GELRVRVSAD KDKGTVTIED NGIGMTRDGV IEHLGTIAKS GTAEFFKNLS GDSAKDSQLI
     GQFGVGFYSA FIVAKRVEVF TRAAGHSADE GVKWESEGEG NFSVETITKA ERGTKIVLHL
     RDEEKEFADD WRLRSIITKY SDHISIPVEM YQEGTPERDG PDGEKIPATE GQWKAMNKAT
     ALWTRSKSDV SDEEYKEFYK HISHDFADPL DWSHNKVEGN QEYTSLLYIP AKAPWDLWNR
     DRKHGLKLFV QRVFIMDDAE QFMPSYLRFV QGLIDSNDLP LNVSREILQD NKVTRNLRQA
     LTKRVLSMLE KLAKDDADKY QQFWAEFGTV LKEGPAEDFA NRERIAGLLR FASTHTGDAT
     PSVSLDDYIG RMKEGQEKIY YIVADSHEAA ANSPHLELLK KKGIEVLLLS ERIDEWLINH
     LHDYKEKALH SVTRGDLDLG ALEDEAEKAA QEKLAQESEP LVERFKSALG DKVSDVKITT
     RLTDTPACVV TGEGEMSSQM IKLMQAAGQP VPESKPTLEL NPTHPLVARL DKEQDETAFA
     EWAEMLLAQA TLSERGSLAD PSAFIKLVNQ MLLKSVG