ID   HTPG_HELAH              Reviewed;         621 AA.
AC   Q17VU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Hac_1509;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(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; AM260522; CAK00229.1; -; Genomic_DNA.
DR   RefSeq; WP_011578316.1; NC_008229.1.
DR   AlphaFoldDB; Q17VU7; -.
DR   SMR; Q17VU7; -.
DR   STRING; 382638.Hac_1509; -.
DR   PRIDE; Q17VU7; -.
DR   EnsemblBacteria; CAK00229; CAK00229; Hac_1509.
DR   KEGG; hac:Hac_1509; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_7; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; HACI382638:HAC_RS06395-MON; -.
DR   Proteomes; UP000000775; 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_1000014924"
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;  71286 MW;  927DA90C755856D1 CRC64;
     MSNQEYTFQT EINQLLDLMI HSMYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLKI
     TPSIHLSFDS QKKTLTIKDN GIGMDKNDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
     QFGVGFYSAF MVAGKIVVQT KKVTSEQAYA WVSDGKGKFE INECIKDEQG TEITLFLKDE
     DANFASRWEI DSIVKKYSEH IPFPIFLTYT DTKMEGEGDH KKEVKEEKCE QINQASALWK
     MNKSELKDKD YKEFYKSFAH DNSEPLSYIH NKVEGSLEYT TLFYIPSVAP FDMFRVDYKS
     GVKLYVKRVF ITDDDKELLP SYLRFIKGVI DSEDLPLNVS REILQQNKIL ANIRSASVKK
     ILGEIEKLSK DNENYHKFYE PFGKVLKEGL YGDFENKEKL LELLRFYSKD KEKLISLKEY
     KENLKENQKS IYYLLGENLD LLKASPILEK YAQKGYDVLL LSDEIDAFVM PSVNEYDKMP
     FRDASHSESL KELGLEEIND EVKNQFKDLI KAFEENLKDE IKGVELSSHL TSAVALIGDE
     QNAMMANLMR QMGQNMPESK KTLELNPNHA ILQKLLKCED KEQMSAFIWL LYDGAKLLEK
     GALKDAKSFN ERLNSVLLKA L