ID   HTPG_PARXL              Reviewed;         634 AA.
AC   Q142T5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-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=Bxeno_A1116;
GN   ORFNames=Bxe_A3329;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE29654.1; -; Genomic_DNA.
DR   RefSeq; WP_011487389.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q142T5; -.
DR   SMR; Q142T5; -.
DR   STRING; 266265.Bxe_A3329; -.
DR   PRIDE; Q142T5; -.
DR   EnsemblBacteria; ABE29654; ABE29654; Bxe_A3329.
DR   KEGG; bxb:DR64_1029; -.
DR   KEGG; bxe:Bxe_A3329; -.
DR   PATRIC; fig|266265.5.peg.1148; -.
DR   eggNOG; COG0326; Bacteria.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001817; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258505"
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..634
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   634 AA;  71623 MW;  7AF346116E67A64C CRC64;
     MAQETMSFQA EVKQLLHLMI HSLYSNKEIF LRELISNASD AADKLRFEAI ENSALYENDP
     NLRIRVSYDK DARTITIDDN GIGMSRDEAI ANLGTIARSG TKEFFGKLSG DQQKDAALIG
     QFGVGFYSGF IVADRITVET RRAGLPASEG VRWESAGEGD FAVEQIERAA RGTTITLHLR
     ADEDELLSSH RLKSIIQKYS DHVALPILMK KEEWDAEKSA MVTKDEDETV NQASALWTRS
     KSDITDEQYK QFYQHLSHDH QDPLTWTHNR VEGRSEYTQL LYVPTHAPFD MFNRDHRGGL
     KLYVKRVFIM DDAEQLLPAY LRFVKGVVDS ADLPLNVSRE ILQESRDVKA IREGVTKRVL
     SMLEDLANSD NEADKEKYAG FWKEFGQVLK EGIGEDFANR ERIAKLLRFA STHTDTPEQT
     VSLADYVARM KPEQTKIYYV TADTWQAATH SPHLEVFRKK GVEVLLLTDR VDEWILSFLT
     EFEGKPLQSV ARGDLDLGAL NDEEKEAQEK VSEEFKPLVE KMKEALKDKA KDVRLTFRLT
     DSPSCLVADD GEMSGYLQRM LKAAGQQAPS FHPILEVNPE HALVKGLHAD SANFDDWCHL
     LFDQALLAEG GALEDPASFV KRTNALLLAR ANEA