ID   HTPG_EHRCJ              Reviewed;         637 AA.
AC   Q3YSL9;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=Ecaj_0237;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68286.1; -; Genomic_DNA.
DR   RefSeq; WP_011304364.1; NC_007354.1.
DR   AlphaFoldDB; Q3YSL9; -.
DR   SMR; Q3YSL9; -.
DR   STRING; 269484.Ecaj_0237; -.
DR   PRIDE; Q3YSL9; -.
DR   EnsemblBacteria; AAZ68286; AAZ68286; Ecaj_0237.
DR   KEGG; ecn:Ecaj_0237; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000435; 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; 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; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224204"
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          335..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          559..637
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   637 AA;  72723 MW;  96EBF42BED5EB620 CRC64;
     MQDVVNSEKL KFDAEVGKVL KLVIHSLYTN KDIFLRELIS NASDACDKLR YESLSNQDLI
     DGDTDFKIVI SVDQDKNRLY ISDNGIGMNR QDLIDNLGTI AHSGTQRFLD AINNETSSQG
     VVELIGKFGV GFYSAFMVAS EVIVESRKAG ESIGYQWRSA GDGEFIISQL EDGQFPRGTK
     ITLILKTEES EFVDKFRIEH IVTTYSYHIN YPVYFLNDAG EEEKLNSDAA IWTKSKDEIS
     AQEHQNFFRS VAHVGGEPWM ILHNKNEGVI EYTNLLYIPS IKPFDLFHPD RKCSVKLYVN
     KVFITEDNVQ IIPQYLRFLK GIIDSSDLPL NISRETLQNN KVIEKIKQSI VKRVLSELKK
     KAENDINDYK KFWENFGSVL KEGLCESMNT EFREELLSAC RFYSTNSDDS LISLEDYIER
     MKEGQDNIYY LTGNDLDSIK KSPQLEGFVS RGIEVILLID PVDDFWTNVV TDYQRVPLKS
     VIRADEDLEK LAHLKKDEEV GESKDENPDS KEKVDAFVKY AIQVLDKLVS GVRVSKKLTN
     SPVCLAVADG SMDIRMERFL REQKQLNYKS TKILEINPKH PIVSRMIDEY ANTGENAVLD
     NMLHLLLGQA CILEGEELED VSSFAERMNN VLVKVYQ