ID   HSP82_MAIZE             Reviewed;         715 AA.
AC   Q08277;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Heat shock protein 82;
GN   Name=HSP82;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf, and Seedling;
RX   PubMed=7683257; DOI=10.1002/dvg.1020140105;
RA   Marrs K.A., Casey E.S., Capitant S.A., Bouchard R.A., Dietrich P.S.,
RA   Mettler I.J., Sinibaldi R.M.;
RT   "Characterization of two maize HSP90 heat shock protein genes: expression
RT   during heat shock, embryogenesis, and pollen development.";
RL   Dev. Genet. 14:27-41(1993).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle that is linked to its ATPase activity. This cycle
CC       probably induces conformational changes in the client proteins, thereby
CC       causing their activation. Interacts dynamically with various co-
CC       chaperones that modulate its substrate recognition, ATPase cycle and
CC       chaperone function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; S59780; AAB26482.2; -; Genomic_DNA.
DR   PIR; A48426; A48426.
DR   AlphaFoldDB; Q08277; -.
DR   SMR; Q08277; -.
DR   STRING; 4577.GRMZM5G833699_P01; -.
DR   PaxDb; Q08277; -.
DR   PRIDE; Q08277; -.
DR   MaizeGDB; 65833; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q08277; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; 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; IPR003594; HATPase_C.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..715
FT                   /note="Heat shock protein 82"
FT                   /id="PRO_0000062950"
FT   REGION          226..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           711..715
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        228..252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   715 AA;  81891 MW;  23EB0F3C46F08739 CRC64;
     MASADVHMAG GAETETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNAS DALDKIRFES
     LTDKSNVNAQ PELFIRLVPD KASKTLSIID SGVGMTKSDL VNNLGTIARS GTKEFMEALA
     AGATDVSMIG QFGVGFYSAY LVADRVMVTT KHNDDEQYVW ESQAGGSFTV THDTTGEQLG
     RGTKITLFLK DDQLEYLEER RLKDLVKKHS EFISYPIYLW TEKTTEKEIS DDEEEEDNKK
     EEEGDVEEVD DEDKDTKDKS KKKKKVKEVS HEWVQINKQK PIWLRKPEEI TRDEYASFYK
     SLTNDWEDHL AVKHFSVEGQ LEFKAILFVP RRAPFDLFDT RKKLNNIKLY VRRVFIMDNC
     EELIPEWLGF VKGVVDSDDL PLNISRETLQ QNKILKVIRK NLVKKCIEMF FEIAENKDDY
     AKFYDAFSKN IKLGIHEDSQ NRAKLADLLR YHSTKSGDET TSLKDYVTRM KEGQKDIYYI
     TGESRKAVEN SPFLERLKKK GYEVLFMVDA IDEYAVGQLK EYDGKKLVSA TKEGLKLDDE
     DDEEAKKRRE ERKKRFEELC KVIKDILGDR VEKVVVSDRI VDSPCCLVTG EYGWTANMER
     IMKAQALRDS SMSAYMSSKK TMEINPDNGI MEELRKRAEA DRNDKSVKDL VLLLFETALL
     TSGFSLDDPN TFAARIHRML KLGLNIDEDA AADEDADMPA LDEGAAEESK MEEVD