ID   HTPG_EHRRG              Reviewed;         637 AA.
AC   Q5FHC4;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
GN   OrderedLocusNames=ERGA_CDS_02450;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(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; CR925677; CAI27697.1; -; Genomic_DNA.
DR   RefSeq; WP_011255411.1; NC_006831.1.
DR   AlphaFoldDB; Q5FHC4; -.
DR   SMR; Q5FHC4; -.
DR   EnsemblBacteria; CAI27697; CAI27697; ERGA_CDS_02450.
DR   GeneID; 56784964; -.
DR   KEGG; erg:ERGA_CDS_02450; -.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; ERUM302409:ERGA_RS01265-MON; -.
DR   Proteomes; UP000000533; 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; Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224205"
FT   REGION          1..335
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          336..559
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          560..637
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   637 AA;  72485 MW;  E7DAF1BF0E67670E CRC64;
     MQGTVNSERL KFDAEVGKVL KLVIHSLYTN KDIFLRELIS NASDACDKLR YQSLSNQDLM
     DAGSELKIVI SVDKDKNRLY ISDNGIGMNR EDLINNLGTI AHSGTQKFLD AINSGASSQQ
     GVVELIGKFG VGFYSAFMVA SEVIVESCKA GESVGYQWKS SGDGEFVISQ LESDQVSRGT
     RITLALKPEE CEFVDKFRIE HIVTTYSYHI NYPVYFLNDK GEEERLNSEA AIWTKAKDEI
     SAEEHQNFFR TVAHVGGEPW MILHNKNEGV IEYTNLLYIP SIKPFDLFHP DRKCSVKLYV
     NKVFITEDNV QIIPQYLRFL KGIIDSSDLP LNISRETLQN NKIIEKIKRS LVKRVLSELK
     KKAESNIEDY TKFWDNFGSV LKEGLCESMN TEFREELISV CRFYSTHSND SLISLEDYIE
     RMKPEQNNIY YLTGNDLDSI KKSPQLEGFV SRGVEVLLLV DPVDDFWTNV VTDYQKVPLR
     SVIRADEDLE KFSDVEKGDE SKDSQNEDTQ SKEKVDKFIG YAAQVLNNLV SNVRVSKKLT
     DSPVCLAVAD GSMDIRMERF LREQKQLNYK STKILEINSK HPIISKMIDQ YTENGESAML
     CNMLHLLLGQ ACILEGEELQ NVSDFAERMN SVLSQIN