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 27-MAR-2024, 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}; OrderedLocusNames=Ecaj_0237;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; 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 KEGG; ecn:Ecaj_0237; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR InParanoid; Q3YSL9; -.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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_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
//
