ID   HTPG_BACTN              Reviewed;         681 AA.
AC   Q8A9B8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=BT_0897;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO76004.1; -; Genomic_DNA.
DR   RefSeq; NP_809810.1; NC_004663.1.
DR   RefSeq; WP_008765725.1; NC_004663.1.
DR   AlphaFoldDB; Q8A9B8; -.
DR   SMR; Q8A9B8; -.
DR   STRING; 226186.BT_0897; -.
DR   PaxDb; Q8A9B8; -.
DR   PRIDE; Q8A9B8; -.
DR   EnsemblBacteria; AAO76004; AAO76004; BT_0897.
DR   GeneID; 60926870; -.
DR   KEGG; bth:BT_0897; -.
DR   PATRIC; fig|226186.12.peg.909; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   InParanoid; Q8A9B8; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
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_0000236984"
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          589..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   681 AA;  78437 MW;  E6B00395AB538163 CRC64;
     MQKGNIGVTT ENIFPIIKKF LYSDHEIFLR ELVSNAVDAT QKLNTLASIG EFKGELGDLT
     IHVELGKDTI TISDRGIGLT AEEIEKYINQ IAFSGANDFL EKYKDDANAI IGHFGLGFYS
     AFMVAKKVEI ITKSYRDEAQ AIKWTCDGSP EFTIEEVDKA DRGSDIILYI DDDCKEFLEE
     ARVSELLKKY CSFLPVPIAF GKKKEWKDGK QIETTEDNII NDTTPLWTRK PSELSDEDYK
     SFYTKLYPMS DEPLFWIHLN VDYPFHLTGI LYFPKVKSNI ELNKNKIQLY CNQVYVTDSV
     EGIVPDFLTL LHGVIDSPDI PLNVSRSYLQ SDSNVKKIST YITKKVSDRL QSIFKNDRKQ
     FEEKWNDLKI FINYGMLTQE DFYEKAQKFA LFTDTDNKHY TFEEYQTLIK DNQTDKDGNL
     IYLYANNKDE QFSYIEAATN KGYNVLLMDG QLDVAMVSML EQKFEKSRFT RVDSDVIDNL
     IIKEDKKNET LEGEKQEAIT TAFKSQLPKM DKVEFNVMTQ ALGDNSAPVM ITQSEYMRRM
     KEMANIQAGM SFYGEMPDMF NLVLNSDHKL IKQVLDEEEA ACHPEVAPIQ TEMNSVSKRR
     NELKDSQKDK KEEDIPTAEK DELNELDKKW DELKNKKEGI FAGYASNNKV IRQLIDLALL
     QNNMLKGEAL NNFVKRSIEL I