ID   HTPG_BACFN              Reviewed;         681 AA.
AC   Q5LCH4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=BF2491;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
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; CR626927; CAH08191.1; -; Genomic_DNA.
DR   RefSeq; WP_005793737.1; NC_003228.3.
DR   AlphaFoldDB; Q5LCH4; -.
DR   SMR; Q5LCH4; -.
DR   STRING; 272559.BF9343_2410; -.
DR   PRIDE; Q5LCH4; -.
DR   EnsemblBacteria; CAH08191; CAH08191; BF9343_2410.
DR   KEGG; bfs:BF9343_2410; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000006731; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..681
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000236983"
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;  77959 MW;  F306316D053831EB 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 EKVEFNVMTQ ALGENGSPVM ITQSEYMRRM
     KEMANIQAGM SFYGEMPDMF NLVLNSDHKL VKEVLADEEK ECSAAIAPIQ TELEDVTKRR
     DALKKKQEGK KDEDIPTAEK DELNDLDKKW DELKQQKDSI FAGYAGKNKV VRQLIDLALL
     QNNMLKGEAL NNFVKRSIEL I