ID   HTPG_HELPH              Reviewed;         621 AA.
AC   Q1CUU4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, 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=HPAG1_0211;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84278.1; -; Genomic_DNA.
DR   RefSeq; WP_000070524.1; NC_008086.1.
DR   AlphaFoldDB; Q1CUU4; -.
DR   SMR; Q1CUU4; -.
DR   EnsemblBacteria; ABF84278; ABF84278; HPAG1_0211.
DR   KEGG; hpa:HPAG1_0211; -.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008835; 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..621
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258513"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..547
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          548..621
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   621 AA;  71333 MW;  D2CAACCCAE5DEC00 CRC64;
     MSNQEYTFQT EINQLLDLMI HSLYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLNI
     TPSIHLSFDS QKKTLTIKDN GIGMDKNDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
     QFGVGFYSAF MVASKIVVQT KKVTNHQAYA WVSDGKGKFE ISECVKEEQG TEITLFLKEE
     DSHFASRWEI DGIVKKYSEH IPFPIFLTYT DTKFEGEGDH KKEVKEEKCD QINQASALWK
     MNKSELKDKD YKDFYQSFAH DNSEPLSYIH NKVEGSLEYT TLFYIPSKAP FDMFRVDYKS
     GVKLYVKRVF ITDDDKELLP SYLRFVKGVI DSEDLPLNVS REILQQNKIL ANIRSASVKK
     ILSEIERLSK DEKNYHKFYE PFGKVLKEGL YGDFENKEKL LELLRFYSKD KEKLISLKEY
     RENLKENQKS IYYLLGENLD LLKASPLLEK YAQKGYDVLL LSDEIDAFVM PGVNEYDKTP
     FRDASHSESL KELGLEEIND EVKDQFKDLM KAFEENLKDE IKGVELSSHL TSAVALIGDE
     QNAMMANFMR QMGQSVPESK KTLELNPNHA ILQKLLKCED KEQLSAFIWL LYDGAKLLEK
     GALKDAKSFN ERLNSVLLKA L