ID   HTPG_RHOP5              Reviewed;         620 AA.
AC   Q07GW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-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=RPE_4897;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
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., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-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; CP000463; ABJ08816.1; -; Genomic_DNA.
DR   RefSeq; WP_011666270.1; NC_008435.1.
DR   AlphaFoldDB; Q07GW8; -.
DR   SMR; Q07GW8; -.
DR   STRING; 316055.RPE_4897; -.
DR   EnsemblBacteria; ABJ08816; ABJ08816; RPE_4897.
DR   KEGG; rpe:RPE_4897; -.
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; 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_1000014943"
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;  68345 MW;  54B4A578D775A601 CRC64;
     MTTTDTAPQT QPFQAEVAEL LNLMVHSVYS ETEIFLRELI SNGSDALDKL RYEAISKPDL
     MEAGGTPKIQ IVPKKAPDTL SVIDNGIGMD RQELIDNLGT IAKSGTKSFL TKLTEAKDGS
     NLIGQFGVGF YAAFMVADRI VVTSRRAGST EAWTWTSSGG AGFEIAPASA EEAERIVRGT
     EIVLHLKPEA AKYLEAYQIE RIVSAYSDNI QFPIELVPEE GEARQINSAS ALWQRSKSEL
     AAEDYKQAYK SIANAFDDPA MTLHYRAEGR YSYAVMLFAP STKPFDLFEP QRKGHVKLYV
     RRVFITDDAD LLPAYLRFIR GVIDSEDLPL NLSREMLQNN PQLVQIRKAV TGKVIGELES
     LGEKDPENFA KIWDAFGPVI KEGIWEDYER REKLLALSRF TTTKGDNRTL KNYVEDLRDN
     QTEIYYLVGD SLERLKSNPK LESAAARGIE VLLLTDPVDA FWTSAPLDFG GKPLKSLSQG
     DVNFDLIPTT DEAKDEQPKP ETDEALVIAT IKDALGERVS DVRASQRLTA SASCLIAGGQ
     GPDRALERML AQQNRGGASK PILEINLRHP LVAAIGRPGN ADAADLSLLL LEQAQILDGE
     LPEDPAGFAG RINRLVLRAL