HTPG_RICCK
ID HTPG_RICCK Reviewed; 623 AA.
AC A8F060;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=A1E_05385;
OS Rickettsia canadensis (strain McKiel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=293613;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=McKiel;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia canadensis.";
RL Submitted (SEP-2007) 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; CP000409; ABV73993.1; -; Genomic_DNA.
DR RefSeq; WP_012149188.1; NC_009879.1.
DR AlphaFoldDB; A8F060; -.
DR SMR; A8F060; -.
DR STRING; 293613.A1E_05385; -.
DR EnsemblBacteria; ABV73993; ABV73993; A1E_05385.
DR KEGG; rcm:A1E_05385; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000007056; 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; 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; Stress response.
FT CHAIN 1..623
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014947"
FT REGION 1..328
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 329..544
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 545..623
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 623 AA; 70809 MW; 569CD318E08A980A CRC64;
MTQEKKKFDA EVGKILNLMI HSLYSNKEIF MRELISNASD ACDKLRYLSQ SNNTLVAGDS
NFKITVKIDK NNGQIIIRDN GIGMNKEDLI ENLGTIARSG TANFLKNLSG DSKKDNMLIG
QFGVGFYSSF MVADKVTVTS RKAGEDKVYV WESDGLGEYI VSNSGKEFTR GTAIVLNIKK
EEDNFLDHFR LKHIVKSYSD HIAVPIYFFD ENGNSEIQLN SASALWTRPK LEITEEQYKE
FYKSLSYTID DPWITLHNKN EGAIEFTNLL FIPSSKTFDL FHPDRKRRVK LYIKRVFISD
ENIDLIPSYL RFLRGVVDSE DLPLNISRES LQHNSILDKI KNAITKRVLA ELKKKKEESP
EDYNKFWSNF GGALKEGLCE STTDHEKLLE VCIFRSALHN KMISLDEYIA NFKEGQNTIY
YLSGDNPDKL LSSPQIEGLL SKNIDVLLFT DTVDDFWVNV NSEYKGHAIK SATRSDIDVE
QTTSSSEEKN TDSKKSDDEY KLLTDYFKET LGDLVKDVKI SKKLTSSPAC LAVSESAMDI
RMERFLIEQK QIANASAKNL ELNPKNKIIE KIFNDLKANN KNNKELVNLI FDQACILEGE
PVADTGAFSK RLNDIVQKAI LSL