ID   HTPG_RHOP2              Reviewed;         628 AA.
AC   Q2IQY5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=RPB_4692;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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; CP000250; ABD09375.1; -; Genomic_DNA.
DR   RefSeq; WP_011443557.1; NC_007778.1.
DR   AlphaFoldDB; Q2IQY5; -.
DR   SMR; Q2IQY5; -.
DR   STRING; 316058.RPB_4692; -.
DR   PRIDE; Q2IQY5; -.
DR   EnsemblBacteria; ABD09375; ABD09375; RPB_4692.
DR   KEGG; rpb:RPB_4692; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000008809; Chromosome.
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..628
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258524"
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          335..550
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          551..628
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   628 AA;  68606 MW;  F1B45D4E35F5AE6F CRC64;
     MTTIDTASET KPFQAEVAEL LNLMVHSVYS ETDIFLRELI SNASDALDKL RYESIANPAL
     MADGGEPKIR IVPKKAPDTL TVIDNGIGMD RQELIDNLGT IAKSGTKSFL TKLTEAKDGA
     GLIGQFGVGF YAAFMVADSI TVTSRRAGSA EAWTWSSSGG AGFEIAPASE EAAARIERGT
     EIVLHLKPDA AKYLEAYQIE RIVSEYSDNI QFPIELVPED GEPRQINSAS ALWQRSKSEL
     TEEDYKQAYK QVAGAFDEPA MTLHYRAEGR QSYAVLLFAP STKPFDLFEP ERKGRVKLYV
     RRVFITADAD LLPPYLRFLR GVIDSEDLPL NLSREMLQNN PQLAQIRKAV TGKVIGELDS
     LADKQPEQFA KIWDAFGPVI KEGLYEDYER REKLLSLARF TTTAGEKRSL AQYVEAMKEN
     QTEIYYLVGD SLDRLKANPK LESAAARGIE VLLLTDAVDA FWTSGGLDFG GKPLKSLSQG
     EVNFDLIPKL DADKAEDKPD EAKADEATVI AVIKDALGDR VSDVKASQRL TASASCLVAG
     GFGPDRELEK MLARANKGAA TKPVLEINLG HPLVAALADT KADKADATDL SFLLLEQAQI
     LDGELPEDPA AFAGRLNRLV LRGVVAHG