ID   HSP82_TOBAC             Reviewed;         499 AA.
AC   P36182;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Heat shock protein 82;
DE   Flags: Fragment;
GN   Name=HSP82;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Samsun;
RA   Severin K., Rottke R., Behrens H., Heller P., Schoeffl F.;
RL   Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases.
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; X63195; CAA44877.1; -; mRNA.
DR   PIR; S18865; S18865.
DR   AlphaFoldDB; P36182; -.
DR   SMR; P36182; -.
DR   STRING; 4097.P36182; -.
DR   PRIDE; P36182; -.
DR   ProMEX; P36182; -.
DR   Proteomes; UP000084051; Unplaced.
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   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           <1..499
FT                   /note="Heat shock protein 82"
FT                   /id="PRO_0000062953"
FT   REGION          15..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           495..499
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        18..38
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   499 AA;  58021 MW;  D7F3C6BC48FEF003 CRC64;
     EFISYPIYLW TEKTTEKEIS DDEDDEPKKD EEGAVEEVDE DKEKEKGKKK KIKEVSHEWQ
     LINKQKPIWL RKPEEITKDE YASFYKSLTN DWEEHLAVKH FSVEGQLEFK AILFVPKRAP
     FDLFDTRKKM NNIKLYVRRV FIMDNCEELI PEYLGFVKGV VDSDDLPLNI SREMLQQNKI
     LKVIRKNLVK KCIEMFNEIA ENKEDYNKFY EAFSKNLKLG IHEDSQNRAK LADLLRYHST
     KSGDEMTSLK DYVTRMKEGQ KDIYYITGES KKAVENSPFL ERLKKKGYEV LYMVDAIDEY
     AVGQLKEYDG KKLVSATKEG LKLDDDSEEE KKKKEEKKKS FENLCKIIKD ILGDKVEKVV
     VSDRIVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMSSY MSSKKTMEIN PDNGIMEELR
     KRAEADKNDK SVKDLVLLLF ETALLTSGFS LDDPNTFAAR IHRMLKLGLS IDEEEEAVED
     ADMPALEETG EESKMEEVD