ID   HTPG_GLUOX              Reviewed;         623 AA.
AC   Q5FS51;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-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=GOX1024;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60795.1; -; Genomic_DNA.
DR   RefSeq; WP_011252588.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FS51; -.
DR   SMR; Q5FS51; -.
DR   STRING; 290633.GOX1024; -.
DR   EnsemblBacteria; AAW60795; AAW60795; GOX1024.
DR   KEGG; gox:GOX1024; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000006375; 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..623
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224209"
FT   REGION          1..336
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          337..546
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          547..623
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   623 AA;  69326 MW;  0E9CC2911CC2A26F CRC64;
     MSETNTQKAA EKHEFSAEVG RLLDLVVHAL YSDREIFLRE LVANAADATD KRRFEALTDS
     ALALPENASI RINPDKSQKE LTISDDGVGM THDELAQNLG TIARSGTRAF GEKLNAAKPE
     DRPSLIGQFG VGFYAAFMVA DRVDVTSRKA GSDEAWTWSS DGKGAFTLTP ASRSTPGTDI
     VLHMKDDADE FLDSWRLRSI IRKWADHISW PITLRETKED GTTEDQAANE GTALWSKPKS
     EITPEQYAEF YRHISHAFDE PYATLHWRAE GVTEFTALLF LPSARPFDFM EQSRESRIHL
     HVRRMFITDE AELVPNWMRF VQGVVDTEDL PLNVSREMLQ ATPVLARIRK AVTKRVLSEI
     SKRAKEADSG FNSFWENFGA VIKEGLWEDA EHRTEIAGFA RFHSTYSDDL ITLDDYISRM
     KDGQDAIYYL TGDSLDALKS SAQLEGFRAR GLEVLLLSDP VDGFWPERLS SYQEKPLRSV
     THSHGDLEKF ESVEADTTEA ADVEKLVPAL KDALGDQVKD VRSTVRLTGS AVVITSDGGP
     DLTMQRLMRR SGQAMPAMPP ILEINPKHPL IKALAERVAK GESVKDYATV LLDLARVQEG
     EPLPDPTGFG RSLATLLAGP AAE