ID   HTPG_BACF6              Reviewed;         681 AA.
AC   E1WNR6; P58476; Q64TM1;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=BF638R_2451;
OS   Bacteroides fragilis (strain 638R).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=862962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=638R;
RX   PubMed=11807048; DOI=10.1128/jb.184.4.895-903.2002;
RA   Smalley D., Rocha E.R., Smith C.J.;
RT   "Aerobic-type ribonucleotide reductase in the anaerobe Bacteroides
RT   fragilis.";
RL   J. Bacteriol. 184:895-903(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638R;
RX   PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA   Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA   Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA   Barron A., Clark L., Bentley S.D., Parkhill J.;
RT   "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT   strain capsule diversity in three strains of Bacteroides fragilis.";
RL   Microbiology 156:3255-3269(2010).
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; AF404759; AAL02103.1; -; Genomic_DNA.
DR   EMBL; FQ312004; CBW22960.1; -; Genomic_DNA.
DR   RefSeq; WP_008768895.1; NC_016776.1.
DR   AlphaFoldDB; E1WNR6; -.
DR   SMR; E1WNR6; -.
DR   PRIDE; E1WNR6; -.
DR   EnsemblBacteria; CBW22960; CBW22960; BF638R_2451.
DR   GeneID; 66328543; -.
DR   KEGG; bfg:BF638R_2451; -.
DR   PATRIC; fig|862962.3.peg.2508; -.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000008560; 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_0000405242"
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"
FT   REGION          601..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  77971 MW;  E88C12B0339F3F1B 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 LFTDTDGKHY TFEEYQTLIK DNQTDKDKNL
     IYLYANNKDE QFAYIEAAKN KGYNVLLMDG QLDVAMVSML EQKLEKSRFT RVDSDVVDNL
     IVKEDKKSDV LEASKQEALS AAFKSQLPKM EKVEFNVMIQ ALGENGSPVM ITQSEYMRRM
     KEMANIQAGM SFYGEMPDMF NLVLNSDHKL VKEVLADEEK ECSAAIAPIQ TELEDVTKRR
     DALKKKQEGK KDEDIPTAEK DELNDLDKKW DELKQQKDSI FAGYAGKNKV VRQLIDLALL
     QNNMLKGEAL NNFVKRSIEL I