ID   HTPG_FRATH              Reviewed;         628 AA.
AC   Q2A5E0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=FTL_0267;
OS   Francisella tularensis subsp. holarctica (strain LVS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=376619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVS;
RA   Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA   Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA   Garcia E.;
RT   "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT   Strain).";
RL   Submitted (MAR-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; AM233362; CAJ78708.1; -; Genomic_DNA.
DR   RefSeq; WP_003014393.1; NZ_CP009694.1.
DR   AlphaFoldDB; Q2A5E0; -.
DR   SMR; Q2A5E0; -.
DR   KEGG; ftl:FTL_0267; -.
DR   OMA; MRRMKEM; -.
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; Stress response.
FT   CHAIN           1..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258512"
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;  72372 MW;  9E936DD06138B42E CRC64;
     MSEKKYTFET EVDKLLHLVI HSLYSNREIF LRELVSNSSD AIEKLRYESI SNAALNEDDT
     DYAIRIDFDK DAKTITVSDN GIGMTEEEVI ENLGTIAKSG TKKFLESLTG DKSKDNELIG
     QFGVGFYSSF IVADKVTVRT RKAGQDKSQA TKWVSDAQNG FTVEIITKEK RGTEVILHIK
     KEHLDLLEYH VLKGLVNKYS DCINTPIQMK KVEYDKDGKQ TVKDEYETVN NTKAIWLRSK
     GEVTNEEYQE FYKYISHDFA DALMWIHNKV EGNLEYNSLL YIPQNKPFDF WNRDKDYGLS
     LYVRRVFIME NKELLPPYLR FVKGVIDSAD LPLNVSREIL QHNKVIDKIK KAITTKILSE
     LKKLASKDKE KYQKFWDSFG QVLKEGVSDD YSNKEKIAGL LRFATTQSGD SKQTVSLADY
     ISRMKESQDT IYYITSDSYK AAANNPQLEA FKKKGIEVIL MTDRIDEWMM STLTEFDDKH
     MKSIIKGDID LDKFETPENK EKFEKEAKDF EKVLKEIKEV LKDKVEDVRL SKRLTDSPSC
     VVVNDYGMSL HMQKMMEEAG QSFMPGMGMK PILELNAEHN LVQKLKNEAD TEIFADLSEL
     LLLQAMFVEG AKIEDPMAFV KLVNKYIR