HTPG_RICB8
ID HTPG_RICB8 Reviewed; 621 AA.
AC A8GWJ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=A1I_04390;
OS Rickettsia bellii (strain OSU 85-389).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=391896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU 85-389;
RA Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT "Complete genome sequencing of Rickettsia bellii.";
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; CP000849; ABV79221.1; -; Genomic_DNA.
DR RefSeq; WP_012151911.1; NC_009883.1.
DR AlphaFoldDB; A8GWJ4; -.
DR SMR; A8GWJ4; -.
DR PRIDE; A8GWJ4; -.
DR KEGG; rbo:A1I_04390; -.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
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..621
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014946"
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 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..621
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT COMPBIAS 481..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 70595 MW; B7A5A501499D7CFD CRC64;
MKQEKKKFDA EVGKILNLMI HSLYSNKEIF MRELISNASD ACDKLRYLSQ SEAELVAGDS
NFKITVKGDK NNGQVIIRDN GIGMNKEDLI ENLGTIARSG TANFLKNLSG DSKKDNMLIG
QFGVGFYSSF MVADKVTVTS RKAGEDKVYV WESEGEGEYI VSNSDREFSR GTEIALHIKK
EEDSFLDHFR LKHIVKSYSD HIAVPIYFFD EGDNNEIQLN SASALWTRSK SEITEEQYKE
FYKSLSYAVD DPWVTMHNKN EGAIEFTNLL FIPSSKTYDL FHPDRKRRVK LYIKRVFISD
ENIDLIPSYL RFLRGVVDSE DLPLNISRES LQHNNVLEKI KNAITKRVLG ELKKKKEDSP
DEYNNFWANF GGALKEGLCE ATTDHEKLLE VCIFRSALHN KMISLDEYIK GFKEGQNTIY
YLSGDNPDKL LSSPQIEGLL SKNIDVLLFT DTVDDFWVNV NSEYKGHAIK SATRSDIDVD
QATSSSEEKN KDDKKSDDEY KSLTDYFKEV LGILVKDVKI SKKLTSSPAC LAVSEAAMDI
RMERFLIEQK QIANASAKNL ELNPKNKIIE KIFNDLKANN KNNEELVKLI FDQACILEGE
PVADTGAFSK RLNDIVQKAI L