ID   HTPG_HELPJ              Reviewed;         621 AA.
AC   Q9ZMM2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 128.
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=jhp_0196;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001439; AAD05780.1; -; Genomic_DNA.
DR   PIR; A71961; A71961.
DR   RefSeq; WP_000070591.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMM2; -.
DR   SMR; Q9ZMM2; -.
DR   STRING; 85963.jhp_0196; -.
DR   EnsemblBacteria; AAD05780; AAD05780; jhp_0196.
DR   KEGG; hpj:jhp_0196; -.
DR   PATRIC; fig|85963.30.peg.824; -.
DR   eggNOG; COG0326; Bacteria.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000804; 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; PF02518; HATPase_c; 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_0000062993"
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;  71140 MW;  3CA62ABDD9796B69 CRC64;
     MSNQEYTFQT EINQLLDLMI HSLYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLNT
     TPSIHLSFDS QKKTLTIKDN GIGMDKSDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
     QFGVGFYSAF MVASKIVVQT KKVTSHQAYA WVSDGKGKFE ISECVKEEQG TEITLFLKEE
     DSHFASRWEI DSVVKKYSEH IPFPIFLTYT DTKFEGEGDN KKEVKEEKCD QINQASALWK
     MNKSELKEKD YKDFYQSFAH DNSEPLSYIH NKVEGSLEYT TLFYIPSKAP FDLFRVDYKS
     GVKLYVKRVF ITDDDKELLP SYLRFVKGVI DSEDLPLNVS REILQQNKIL ANIRSASVKK
     ILSEIERLSK DNKNYHKFYE PFGKVLKEGL YGDFENKEKL LELLRFYSKD KGEWISLKEY
     KENLKENQKS IYYLLGENLD LLKASPLLEK YAQKGYDVLL LSDEIDAFVM PGVNEYDKTP
     FRDASHSESL KELGLAEIHD EVKDQFKDLI KAFEENLKDE IKGVELSGHL TSAVALIGDE
     PNAMMANWMR QMGQSVPESK KTLELNPNHA ILQKLLKCED KEQLSAFIWL LYDGAKLLEK
     GALKDAKSFN ERLNSVLLKA L