ID   HTPG_BURP6              Reviewed;         632 AA.
AC   A3N786;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
GN   OrderedLocusNames=BURPS668_1158;
OS   Burkholderia pseudomallei (strain 668).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=668;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000570; ABN82482.1; -; Genomic_DNA.
DR   RefSeq; WP_011851280.1; NC_009074.1.
DR   AlphaFoldDB; A3N786; -.
DR   SMR; A3N786; -.
DR   EnsemblBacteria; ABN82482; ABN82482; BURPS668_1158.
DR   KEGG; bpd:BURPS668_1158; -.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002153; 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_1000014905"
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;  71163 MW;  2D98C2DEBEDCBD7E CRC64;
     MTQQTMSFQA EVKQLLHLMI HSLYSNKEIF LRELVSNASD AADKLRFEAL ENNALYESDP
     NLRIRLSFDK AARTITIDDN GIGMSRDEAI ANLGTIARSG TKEFFSKLSG DQQKDAALIG
     QFGVGFYSGF IVADRITVET RRAGLPASEG VRWESAGEGD FQVDTIERAA RGTTITLHLR
     EGEDELLSSY RLKSIVQKYS DHVALPILMK KEEWDQEKGE MVEKDEDETI NQASALWTRA
     KSEVTDEQYK QFYQHVAHDH QDPLAWTHNR VEGRSEYTQL LFVPSHAPFD LWNRDYRGGL
     KLYVKRVFIM DDAEQLLPQY LRFIKGVVDS SDLPLNVSRE ILQESRDVKA IREGVTKRAL
     SMLEELANAE DDAGKEKYKT FWSAFGQVLK EGIGEDHANR ERVAKLLRFA STHGDTDAQD
     VALADYVARM KPEQTKIYYV TADTWQAAKN SPHLEVFRKK GVEVLLLTDR VDEWMLSFLH
     EFDGKPLASV ARGDLDLGAL NDDEKKAQEE TGEAMKPVVD KMKETLGEKV KDVRVTFRLT
     DSPSCLVADD NDMSGYLQRM LKAAGQSAPS FQPILEINPE HPLVKALKAD GADFGDWCHL
     LFDQALLAEG GALEDPASFV KRTNALLLSR AA