ID   HTPG_DECAR              Reviewed;         636 AA.
AC   Q47GZ8;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=Daro_1127;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
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; CP000089; AAZ45883.1; -; Genomic_DNA.
DR   RefSeq; WP_011286892.1; NC_007298.1.
DR   AlphaFoldDB; Q47GZ8; -.
DR   SMR; Q47GZ8; -.
DR   STRING; 159087.Daro_1127; -.
DR   EnsemblBacteria; AAZ45883; AAZ45883; Daro_1127.
DR   KEGG; dar:Daro_1127; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_4; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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..636
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224203"
FT   REGION          1..345
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          346..562
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          563..636
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   636 AA;  71568 MW;  C03CD44CEA740DF7 CRC64;
     MSESATANAN RETLGFQAEV KQLLQLMIHS LYSNKEIFLR ELVSNASDAC DKLRFEALNN
     SALYGDDSEL KIRIAFDKDA RTITISDNGI GLSRDEAVEH LGTIAKSGTK EFFSALTGDQ
     AKDAHLIGQF GVGFYSSFII ADKVTVVSRR AGVEANQAVC WESGGEGDYT VEMVEKATRG
     TDVTLHLREG EDEFLGGWKL KSIIRKYSDH ITLPIVMKKE DWKDGEQVMT EEDETVNQAN
     ALWVRSKSDI TEEQYKEFYK HVAHDFEDPL AWTHARVEGK QEYTQLLYIP ARAPFDLWDR
     NARHGIKLYV RRVFIMDDAE QLMPLYMRFV RGVVDSSDLP LNVSREILQQ SKDIDGIRSG
     CTRKVLGMLE DLAENDKEKY AKFWEAFGSV LKEGVGEDHA NKEKIAGLIR FSSTHNDTAE
     QNVSLADYIG RMKEGQEKIY FVTADTFNAA KNSPHLEIFR KKGIEVLLLS DRVDEWVVGH
     LTEFDGKHLQ SVAKGGLDLG KLEDEAEKQE AEKAADDYKE LLEKVKTSLG DKVKDVRVTY
     RLTDSPSCLV SDEHDPSGNL ARLMKAAGQP MPNSKPILEI NPQHPAVMRL KYEESRFDDW
     AALLFEQATL AEGGQLDDPA GFVKRINDLM MALSAK