ID   HSP83_IPONI             Reviewed;         703 AA.
AC   P51819;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Heat shock protein 83;
GN   Name=HSP83A;
OS   Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=35883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Cotyledon;
RX   PubMed=16653195; DOI=10.1104/pp.100.4.1764;
RA   Felsheim R.F., Das A.;
RT   "Structure and expression of a heat shock protein 83 (hsp83) gene of
RT   Pharbitis nil.";
RL   Plant Physiol. 100:1764-1771(1992).
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   -!- INDUCTION: By heat shock and light. This heat shock protein is induced
CC       by light only after a prolonged dark period or vice versa.
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; M99431; AAA33748.1; -; Genomic_DNA.
DR   RefSeq; XP_019149680.1; XM_019294135.1.
DR   AlphaFoldDB; P51819; -.
DR   SMR; P51819; -.
DR   PRIDE; P51819; -.
DR   GeneID; 109146489; -.
DR   KEGG; ini:109146489; -.
DR   OrthoDB; 924636at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..703
FT                   /note="Heat shock protein 83"
FT                   /id="PRO_0000062954"
FT   REGION          220..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           699..703
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        222..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..703
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   703 AA;  80821 MW;  C8E5DC10586AB736 CRC64;
     MADVQMAEAE TFAFQAEINQ LLSLIINTFY SNKEIFLREL ISNASDALDK IRFESLTDKS
     KLDAQPELFI RLVPDKTNKT LSIIDSGVGM AKADLVNNLG TIARSGTKEF MEALQAGADV
     SMIGQFGVGF YSAYLVAEKV IVTTKHNDDE QYIWESQAGG SFTVTRDVDG EQLGRGTKIT
     LFLKEDQLEY LEERRIKDLV KKHSEFISYP IYLWTEKTTE KEISDDEDDE PKKEEEGDIE
     EVDEDKEKEG KKKKKIKEVS HEWQLINKQK PIWLRKPEEI TKEEYASFYK SLTNDWEDHL
     AVKHFSVEGQ LEFKAILFVP KRAPFDLFDT RKKMNNIKLY VRRVFIMDNC EELIPEYLGF
     VKGVVDSDDL PLNISREMLQ QNKILKVIRK NLVKKCIEMF NEIAENKDDY NKFYEAFSKN
     LKLGIHEDSQ NRAKLADLLR YYSTKSGDEL TSLKDYVTRM KEGQKDIYYI TGESKKAVEN
     SPFLERLKKK GYEVLFMVDA IDEYAVGQLK EYDGKKLVSA TKEGLKLEDD DEEEKKKREE
     KKKSFENLCK IIKDILGDKV EKVVVSDRIV DSPCCLVTGE YGWTANMERI MKAQALRDSS
     MSSYMSSKKT MEINPDNGIM EELRKRAEAD KNDKSVKDLV LLLFETALLT SGFSLDDPNT
     FGARIHRMLK LGLSIDEEEA GDDADMPALE EEAGEESKME EVD