ID   HTPG_FRATN              Reviewed;         628 AA.
AC   A0Q4L0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=FTN_0266;
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA   Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA   Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA   Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA   Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA   Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary events
RT   associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(2007).
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; CP000439; ABK89175.1; -; Genomic_DNA.
DR   RefSeq; WP_003038264.1; NZ_CP009633.1.
DR   AlphaFoldDB; A0Q4L0; -.
DR   SMR; A0Q4L0; -.
DR   EnsemblBacteria; ABK89175; ABK89175; FTN_0266.
DR   GeneID; 60805849; -.
DR   KEGG; ftn:FTN_0266; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; FTUL401614:G1G75-277-MON; -.
DR   Proteomes; UP000000762; 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; Stress response.
FT   CHAIN           1..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014918"
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;  72331 MW;  3C920A8FD1558380 CRC64;
     MSEKKYTFET EVDKLLHLVI HSLYSNREIF LRELVSNSSD AIEKLRYESI SNAALNEDDT
     DYAIRIDFDK DAKTITVSDN GIGMTEEEVI ENLGTIAKSG TKKFLESLTG DKSKDNELIG
     QFGVGFYSSF IVADKVTVRT RKAGQDKSQA TKWVSDAQNG FTVETITKEK RGTEVILHIK
     KEHLDLLEYH VLKGLVNKYS DCINTPIQMK 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 LDKFETPENK EKFEKETKDF EKVLKEIKEV LKDKVEDVRL SKRLTDSPSC
     VVVNDYGMSL HMQKMMEEAG QGFMPGMGMK PILELNAEHN LVQKLKNEAD TEIFADLSEL
     LLLQAMFVEG AKIEDPMAFV KLVNKYIR