ID   HTPG_ROSDO              Reviewed;         621 AA.
AC   Q162C5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=RD1_3696;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG33168.1; -; Genomic_DNA.
DR   RefSeq; WP_011569779.1; NZ_FOOO01000012.1.
DR   AlphaFoldDB; Q162C5; -.
DR   SMR; Q162C5; -.
DR   STRING; 375451.RD1_3696; -.
DR   EnsemblBacteria; ABG33168; ABG33168; RD1_3696.
DR   KEGG; rde:RD1_3696; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000007029; 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; 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..621
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258526"
FT   REGION          1..325
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          326..541
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          542..621
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   621 AA;  68991 MW;  9437891C9B189786 CRC64;
     MTDASVKETF SFQTEVGQLL DIVAGSLYSN REIFLRELVS NASDACDKLR YEALTNPSLA
     QNADEFAISL AVDKKAKTLS VSDNGIGMNH GDLLDTLGTI ARSGTGAFLD ALKSEEKGDI
     GLIGQFGVGF YSAFMVAERV DVLTRKAGED ESWLWSSDGK GEFSIEPGER AQSGTTVTLH
     LKKDAKEFLE ESRIRHIIKT YSEHISFPVR LDTEALNSAS AIWTRAPKEI TEEQHTEFYH
     HVSNAFDKPW HVLHNRVEGT VNHTSLLYVP SMAPFDLYEA ERKSHVKLYV NRVFISDNTR
     DLIPAYLRFL RGVVDSQDLS LNVSREMLQS DPKLAKIKTS VTKKVLSELK KKAKKSPEDY
     AGFWQNFGPV LKEGLIEDPA LRDRILEICR FSSTKSGDVT SLADYISRCK EGQDAIYYIA
     GDDARKIAQS PHLEGFRAKD VEVLLLSDHV DEFWLQHITE FEGKPFKSIT RGAADLDKIN
     EGEKADDAEE EAQAPDLNDL IAALKLELGA SVKDVRPSKR LTDSPVCLIA DEGDIDVNLE
     RMLKRHGQLQ DAMPRVLELN PDHRIITKLA ERAKGSAAAS DTLLKDAAHL LLDQARIADG
     ETPADPAEFV RRLGSVMDSA L