ID   HTPG_FRATT              Reviewed;         628 AA.
AC   Q5NHT8;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=FTT_0356;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG44989.1; -; Genomic_DNA.
DR   RefSeq; WP_003020060.1; NZ_CP010290.1.
DR   RefSeq; YP_169404.1; NC_006570.2.
DR   AlphaFoldDB; Q5NHT8; -.
DR   SMR; Q5NHT8; -.
DR   IntAct; Q5NHT8; 23.
DR   MINT; Q5NHT8; -.
DR   STRING; 177416.FTT_0356; -.
DR   DNASU; 3191490; -.
DR   EnsemblBacteria; CAG44989; CAG44989; FTT_0356.
DR   KEGG; ftu:FTT_0356; -.
DR   eggNOG; COG0326; Bacteria.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001174; 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; 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..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224208"
FT   REGION          1..337
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          338..554
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          555..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  72349 MW;  2496B9EC4F230DAC CRC64;
     MSEKKYTFET EVDKLLHLVI HSLYSNREIF LRELVSNSSD AIEKLRYESI SNAALNEDDT
     DYAIRIDFDK DAKTITVSDN GIGMTEEEVI ENLGTIAKSG TKKFLESLTG DKSKDNELIG
     QFGVGFYSSF IVADKVTVRT RKAGQDKSQA TKWVSDAQNG FTVETITKEK RGTEVILHIK
     KEHLDLLEYH VLKGLVNKYS DCINTSIQMK KVEYDKDGKQ TVKDEYETVN NTKAIWLRSK
     DEVTDEEYQE FYKYISHDFA DALMWIHNKV EGNLEYNSLL YIPQNKPFDF WNRDKDYGLS
     LYVRRVFIME NKELLPPYLR FVKGVIDSAD LPLNVSREIL QHNKVIDKIK KAITTKILSE
     LKKLASKDKE KYQKFWDSFG QVLKEGVSDD YSNKEKIAGL LRFATTQSGD SKQTVSLADY
     ISRMKEGQDT IYYITSDSYK AAANNPQLEA FKKKGIEVIL MTDRIDEWMM STLTEFDGKH
     MKSIIKGDID LDRFETPENK EKFEKEAKDF EKVLKEIKEV LKDKVEDVRL SKRLTDSPSC
     VVVNDYGMSL HMQKMMEEAG QSFMPGMGMK PILELNAEHN LVQKLKNEAD TEIFADLSEL
     LLLQAMFVEG AKIEDPMAFV KLVNKYIR