ID   HTPG_BACFR              Reviewed;         681 AA.
AC   P0CJ84; P58476; Q64TM1;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Chaperone protein htpG;
DE   AltName: Full=Heat shock protein htpG;
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=BF2409;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006841; BAD49158.1; -; Genomic_DNA.
DR   RefSeq; WP_011202859.1; NC_006347.1.
DR   RefSeq; YP_099692.1; NC_006347.1.
DR   AlphaFoldDB; P0CJ84; -.
DR   SMR; P0CJ84; -.
DR   STRING; 295405.BF2409; -.
DR   EnsemblBacteria; BAD49158; BAD49158; BF2409.
DR   KEGG; bfr:BF2409; -.
DR   PATRIC; fig|295405.11.peg.2327; -.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002197; 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; 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..681
FT                   /note="Chaperone protein htpG"
FT                   /id="PRO_0000062966"
FT   REGION          1..326
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          327..545
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          546..681
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   681 AA;  78013 MW;  19E32A36007D3AF7 CRC64;
     MQKGNIGVTT ENIFPIIKKF LYSDHEIFLR ELVSNAVDAT QKLNTLASIS EFKGELGDLT
     VHVSLGKDTI TISDRGIGLT AEEIDKYINQ IAFSGANDFL EKYKNDANAI IGHFGLGFYS
     AFMVSKKVEI ITKSYKEGAQ AVKWTCDGSP EFTLEEVEKA DRGTDIVLYI DDDCKEFLEE
     SRISALLKKY CSFLPVPIAF GKKKEWKDGK QVETAEDNVI NDTIPLWTKK PSELSDEDYK
     KFYRELYPMS DEPLFWIHLN VDYPFHLTGI LYFPKVKSNI DLNKNKIQLY CNQVYVTDSV
     EGIVPDFLTL LHGVLDSPDI PLNVSRSYLQ SDSNVKKIST YISKKVSDRL QSIFKNDRAQ
     FEEKWNDLKI FINYGMLTQE DFYDKAQKFA LFTDTDGKYY TFEEYQTLIK DNQTDKDKNL
     IYLYANNKDE QFAYIEAAKN KGYNVLLMDG QLDVAMVSML EQKLEKSRFT RVDSDVVDNL
     IVKEDKKSDV LEASKQEALS AAFKSQLPKM EKVEFNVMTQ ALGENGSPVM ITQSEYMRRM
     KEMANIQAGM SFYGEMPDMF NLVLNSDHKL VKEVLADEEK ECSAAIAPIQ TELEDVTKRR
     DALKKKQEGK KDEDIPTVEK DELNDLDKKW DELKQQKDSI FAGYAGKNKV VRQLIDLALL
     QNNMLKGEAL NNFVKRSIEL I