ID   HTPG_BURL3              Reviewed;         632 AA.
AC   Q39E36;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Bcep18194_A5686;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000151; ABB09280.1; -; Genomic_DNA.
DR   RefSeq; WP_011352806.1; NC_007510.1.
DR   AlphaFoldDB; Q39E36; -.
DR   SMR; Q39E36; -.
DR   EnsemblBacteria; ABB09280; ABB09280; Bcep18194_A5686.
DR   GeneID; 45095573; -.
DR   KEGG; bur:Bcep18194_A5686; -.
DR   PATRIC; fig|482957.22.peg.2663; -.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000002705; 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_0000236987"
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;  71180 MW;  5972E5FEB93D5C9D CRC64;
     MAHETMSFQA EVKQLLHLMI HSLYSNKEIF LRELVSNASD AADKLRFEGL ADNALYEDDP
     NVRIRIGYDK AARTITIDDN GIGMSRDEAI ANLGTIARSG TKEFFTKLSG DQQKDAALIG
     QFGVGFYSGF IVADKITVET RRAGLPASEA VRWESAGEGD FTIDAIERAQ RGTTITLHLR
     EGEDELLSSH RLQSIIQKYS DHIALPILMQ KEEWDQEKGE MVLKDEDETV NQASALWTRS
     KSEVSDEQYT QFYQHIAHDH QDPLTWTHNR VEGRSEYTQL LFVPSHAPFD MWNRDYRGGL
     KLYVKRVFIM DDAEQLLPQY LRFVKGVVDS ADLPLNVSRE ILQESRDVKA IREGVTKRAL
     SMLEELANAE EDAGKEKYKT FWGAFGQVLK EGLGEDHANR ERIAKLLRFA STHGDTDAQD
     VSLADYVSRM KPEQSRIYYV TADAWQAAKN SPHLEVFRKK GVEVLLLTDR VDEWMLSFLQ
     EFDGKPLASV ARGDLDLGEL NDEEKKAQEE AGEAIKPVVE KMKEALGDKV KEVRVTFRLT
     DSPSCLVADD NDMSGYLQRM LKAAGQNAPA MQPILEINPE HALVKQLKAD SADFGDWCHL
     LFDQALLAEG GMLDDPASFV KRTNALLLSR AA