ID   HTPG_BURTA              Reviewed;         632 AA.
AC   Q2SZZ0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BTH_I0955;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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; CP000086; ABC38457.1; -; Genomic_DNA.
DR   RefSeq; WP_009892368.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SZZ0; -.
DR   SMR; Q2SZZ0; -.
DR   PRIDE; Q2SZZ0; -.
DR   EnsemblBacteria; ABC38457; ABC38457; BTH_I0955.
DR   GeneID; 66546542; -.
DR   KEGG; bte:BTH_I0955; -.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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..632
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236988"
FT   REGION          1..339
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          340..559
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          560..632
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   632 AA;  71021 MW;  85D254B5CA429518 CRC64;
     MTQQTMSFQA EVKQLLHLMI HSLYSNKEIF LRELVSNASD AADKLRFEAL ENNALYESDP
     NLRIRLSFDK AARTLTIDDN GIGMSRDEAI ANLGTIARSG TKEFFSKLSG DQQKDAALIG
     QFGVGFYSGF IVADKITVET RRAGLPASEG VRWESAGEGD FSVDTIERAA RGTTITLHLR
     EGEDELLSSY RLKSIVQKYS DHVALPILMK KEEWDQEKGE MVEKDEDETV NQASALWTRA
     KSDVTEEQYK QFYQHVAHDH QDPLAWTHNR VEGRSEYTQL LFVPSHAPFD LWNRDYRGGL
     KLYVKRVFIM DDAEQLLPQY LRFIKGVVDS SDLPLNVSRE ILQESRDVKA IREGVTKRAL
     SMLEELANAE DDAGKEKYKT FWSAFGQVLK EGVGEDHANR ERVAKLLRFA STHGDTDAQD
     VALADYVARM KPEQTKIYYV TADTWQAAKN SPHLEVFRKK GVEVLLLTDR VDEWMLSFLH
     EFDGKPLASV ARGDLDLGAL NDDEKKAQEE TGEAMKPVVD KMKETLGGKV KDVRVTFRLT
     DSPSCLVADD NDMSGYLQRM LKAAGQNAPS FQPILEINPE HPLVKALKAD GADFGDWCHL
     LFDQALLAEG GALEDPASFV KRTNALLLSR AA