ID   HTPG_HELHP              Reviewed;         618 AA.
AC   Q7VFD7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=HH_1740;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP78337.1; -; Genomic_DNA.
DR   RefSeq; WP_011116579.1; NC_004917.1.
DR   AlphaFoldDB; Q7VFD7; -.
DR   SMR; Q7VFD7; -.
DR   STRING; 235279.HH_1740; -.
DR   PRIDE; Q7VFD7; -.
DR   EnsemblBacteria; AAP78337; AAP78337; HH_1740.
DR   KEGG; hhe:HH_1740; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002495; 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..618
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062991"
FT   REGION          1..340
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          341..545
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          546..618
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   618 AA;  70299 MW;  1C1EE2B13FE66E45 CRC64;
     MATKHQFQTE ITQLLDLMIH SLYSHKEIFL RELISNASDA LDKLSYLTLT QENLKTLSFE
     PRIDISFDEE KKTITIEDNG IGMNENDMKE HLGIIAKSGT KSFLSQLSGD KKKDSALIGQ
     FGVGFYSAFM VAHRVVVQSK KAGEEKAYAW VSEGKGEYEI GECVKESQGT QITLYLREED
     AHFASRWEIE GIIHKYSEHI AFPIYLAFVE SKFEGEGENK KEIKENKQSQ INTAKALWKI
     PKAELKDTDY KEFYATLSHD NNEPMRWIHT KVEGNLEYTT LFYIPQKAPF DLFRVDYQSG
     VKLYVKRVFI TDDDKELLPP YLRFVRGVID SEDLPLNVSR EILQQNKILA NIKSASTKKI
     LSEITNIAKN EADYKTFYEQ FGKVLKEGLY GDYENKEKIL ELLRFDSFKS EYISLKAYKE
     SMGNEQKSIY YMLGENKDAL KNAPLLEKFA QKGFDVLLLS DEIDAIVMPM VGEYDKVPLK
     SINSKEALAE LGEESIDEAT QNAYEPLIKG FKDALGEQIA EVKLSSLGDA PLTLIKEDNN
     PMMANLMAQM GQKVPETKPI LQLNITHPLF EKLKTAQEDK IKQSALLLFG AALILEGSTL
     KNAKDFNTEL NSLLLQSL