ID   HTPG_BURMA              Reviewed;         632 AA.
AC   Q62ID1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=BMA1947;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU49908.1; -; Genomic_DNA.
DR   RefSeq; WP_004185742.1; NC_006348.1.
DR   RefSeq; YP_103539.1; NC_006348.1.
DR   AlphaFoldDB; Q62ID1; -.
DR   SMR; Q62ID1; -.
DR   STRING; 243160.BMA1947; -.
DR   EnsemblBacteria; AAU49908; AAU49908; BMA1947.
DR   GeneID; 56595034; -.
DR   KEGG; bma:BMA1947; -.
DR   PATRIC; fig|243160.12.peg.2014; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000006693; Chromosome 1.
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_0000224199"
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;  71149 MW;  F1E905CAD36A6615 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 EGVGEDHANR ERVAKLLRFA STHGDTDAQD
     VALADYVARM KPEQTKIYYV TADTWQAAKN SPHLEVFRKK GVEVLLLTDR VDEWMLSFLH
     EFDGKPLASV ARGDLDLGAL NDDEKKAQEE TGEAMKPVVD KMKETLGEKV KDVRVTFRLT
     DSPSCLVADD NDMSGYLQRM LKAAGQSAPS FQPILEINPE HPLVKALKAD GADFGDWCHL
     LFDQALLAEG GALEDPASFV KRTNALLLSR AA