ID   HTPG_BURCM              Reviewed;         632 AA.
AC   Q0BD34;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Bamb_2383;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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; CP000440; ABI87939.1; -; Genomic_DNA.
DR   RefSeq; WP_011657562.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BD34; -.
DR   SMR; Q0BD34; -.
DR   STRING; 339670.Bamb_2383; -.
DR   EnsemblBacteria; ABI87939; ABI87939; Bamb_2383.
DR   GeneID; 44693052; -.
DR   KEGG; bam:Bamb_2383; -.
DR   PATRIC; fig|339670.21.peg.2539; -.
DR   eggNOG; COG0326; Bacteria.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000662; 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_1000014900"
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;  71182 MW;  5C1A53A4D4216E8D CRC64;
     MAHETMSFQA EVKQLLHLMI HSLYSNKEIF LRELVSNASD AADKLRFEGL ADNALYENDP
     NLRIRIGFDK AARTITIDDN GIGMSRDEAI ANLGTIARSG TKEFFTKLSG DQQKDAALIG
     QFGVGFYSGF IVADKITVET RRAGLPANEA VRWESAGEGD FTIDAIERAQ RGTTITLHLR
     EGEDELLSSH RLKSIIQKYS DHIALPILMQ KEEWDQEKGE MVLKDEDETV NQASALWTRS
     KSDITDEQYT QFYQHVAHDH QDPLTWTHNR VEGRSEYTQL LFVPAHAPFD LWNRDYRGGL
     KLYVKRVFIM DDAEQLLPQY LRFVKGVVDS ADLPLNVSRE ILQESRDVKA IREGVTKRAL
     SMLEELANAE EEAGKEKYKT FWSAFGQVLK EGLGEDHANR ERIAKLLRFA STHGDTDAQD
     VSLADYVSRM KPEQSKIYYV TADTWQAAKN SPHLEVFRKK GVEVLLLTDR VDEWMLSFLH
     EFDGKPLASV ARGDLDLGEL NDEEKKAQEQ AGEAIKPVVE KMKEALGDKV KEVRVTFRLT
     DSPSCLVADD NDMSGYLQRM LKAAGQNAPA MQPILEINPE HALVKQLNAD SASFGDWCHL
     LFDQALLAEG GMLDDPASFV KRTNALLLSR AA