ID   HTPG_RHOPB              Reviewed;         620 AA.
AC   Q20WN5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=RPC_4929;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-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; CP000301; ABD90451.1; -; Genomic_DNA.
DR   RefSeq; WP_011475327.1; NC_007925.1.
DR   AlphaFoldDB; Q20WN5; -.
DR   SMR; Q20WN5; -.
DR   STRING; 316056.RPC_4929; -.
DR   EnsemblBacteria; ABD90451; ABD90451; RPC_4929.
DR   KEGG; rpc:RPC_4929; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258523"
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          335..548
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          549..620
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   620 AA;  68213 MW;  C2BD8F3FD652AD82 CRC64;
     MTTTDTAPQS QPFQAEVAEL LNLMVHSVYS ETDIFLRELI SNASDALDKL RYESIAKPEL
     MADGGEPKIR ILPKKEPDTL SVIDNGLGMD RQELIDNLGT IAKSGTKSFL TKLTEAKDGA
     GLIGQFGVGF YAAFMVADRI VVTSRRARSA EAWTWSSSGG AGFEIAPASE EDAARVTRGT
     EIVLHLKKDA AKYLEPYEIE RVVGAYSDNI QFPIELVPEE GEPRQINSAS ALWQRSKSEL
     TAEDYSQAYK QIAGAFDEPA MTLHYRAEGR YSYAVLLFAP STKPFDLFEP ARKGRVKLYV
     RRVFITDEAD LLPSYLRFIR GVIDSEDLPL NLSREMLQNN PQLAQIRKAV TGKVIGELES
     LGDKDPEAFG KIWDAFGLVI KEGIWEDYER RDKLLALSRF TTTKGENRTL KQYVEDLKEN
     QTEIYYLVGD SIERLKSNPK LESAAARGIE VLLLTDPVDA FWTSAPLDFG GKPLKSLSQG
     DVDFGQIPTT EENKDEQAKP ETDEALTIAA IKDALGDKVS DVRASQRLTA SASCLVAGGL
     GPDRALERML AQQNRGAASK PILEVNLRHP IVAAVAKANA ADAADLSLLL LEQAQILDGE
     LPEDPAAFSA RLNRLVLRAL