ID   HTPG_BUCAP              Reviewed;         625 AA.
AC   Q8K981;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=BUsg_468;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM68011.1; -; Genomic_DNA.
DR   RefSeq; WP_011053978.1; NC_004061.1.
DR   AlphaFoldDB; Q8K981; -.
DR   SMR; Q8K981; -.
DR   STRING; 198804.BUsg_468; -.
DR   PRIDE; Q8K981; -.
DR   EnsemblBacteria; AAM68011; AAM68011; BUsg_468.
DR   KEGG; bas:BUsg_468; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000416; 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; 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..625
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062976"
FT   REGION          1..337
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          338..552
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          553..625
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   625 AA;  72765 MW;  781AB7DCFA801503 CRC64;
     MNIQKKEVYS FQSEVKQLLH LMIHSLYSNK EIFLRELISN ASDAIDKLRF QSISNPELYE
     NDSDFKIQIS INKSQGTLII SDNGIGMTRQ DVVENLGTIA KSGTKSFIKS LEKKEKNVKN
     ELIGEFGVGF YSSFIVSKKV SVRTRFAGSK SNLGVLWESS GEGEYNITDI KKKTRGTEIT
     LFLKKEEEEF LELWRIEGIV SKYSDHITVP VKIQKYDEKN KIYFWEKINK AKALWTQNKA
     TISEKEYQEF YKHLTNDQNN PLFWSHNHVE GINEYISLLF IPEKAAWDIW NRDNKSGLKL
     YVKRVYIMDN SQAFLPNYLR FIRGLIDSNN LPLNVSREIL QDNSITQNLK KALIKRSLKM
     LQTLSKKDNE KYQIFWNQFG SVLKEGPAED SNNLNLIASL LRFTSIQNNS SEQNISLEKY
     ISNMHEKQEK IYYITADSYT SAKNSPHLEL FNKKNIDVLL LSDRIDEWMM NYLTEFEGKK
     FQSISKEDLS LNKLTKENEN KKETSTEMIE FLKKVKKTLG DKVKSVRLTY RLTETPCIVL
     SDSNEMSTQM AKLFSAAGQS VPELKYIFEI NPEHKLIQKI CKIKENEKFD EWIKLLLDQA
     LFAEKGNLEN PHEFIARTNK LILEQ