ID   HSP83_LEIDO             Reviewed;         452 AA.
AC   P27890;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Heat shock protein 83;
DE            Short=HSP 83;
DE   AltName: Full=HSP 90;
DE   Flags: Fragment;
GN   Name=HSP83; Synonyms=HSP90;
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sudan S1;
RX   PubMed=1537901; DOI=10.1128/jcm.30.2.330-335.1992;
RA   de Andrade C.R., Kirchhoff L.V., Donelson J.E., Otsu K.;
RT   "Recombinant Leishmania Hsp90 and Hsp70 are recognized by sera from
RT   visceral leishmaniasis patients but not Chagas' disease patients.";
RL   J. Clin. Microbiol. 30:330-335(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:0000250}.
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; M73492; AAA29252.1; -; mRNA.
DR   PIR; A44888; A44888.
DR   AlphaFoldDB; P27890; -.
DR   SMR; P27890; -.
DR   VEuPathDB; TriTrypDB:LdBPK_330360.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_330008800; -.
DR   VEuPathDB; TriTrypDB:LDHU3_33.0550; -.
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   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; Stress response.
FT   CHAIN           <1..452
FT                   /note="Heat shock protein 83"
FT                   /id="PRO_0000062940"
FT   MOTIF           448..452
FT                   /note="TPR repeat-binding"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   452 AA;  52691 MW;  374A4E2AABFE1966 CRC64;
     TKKVKEVTKE YEVQNKHKPL WTRDPKDVTK EEYAAFYKAI SNDWEDPMAT KHFSVEGQLE
     FRSIMFVPKR APFDMFEPNK KRNNIKLYVR RVFIMDNCED LCPDWLGFVK GVVDSEDLPL
     NISRENLQQN KILKVIRKNI VKKCLEMFDE VAENKEDYKQ FYEQFGKNIK LGIHEDTANP
     KKLMEFLRFY STESGLEMTT LKDYVTRMKE GQKSIYYITG DSKKKLESSP FIEQARRRGL
     EVLFMTEPID EYVMQQVKDF EDKKFACLTK EGVHFEESEE EKQQREEEKA ACEKRCKTMK
     EVLGDKVEKV TVSDRLSTSP CILVTSEFGW SAHMEQIMRN QAVRDSSMSA YMMSKKTMEL
     NPRHPIIKVL RRRVEADEND KAVKDLVFLL FDTSLLTSGF QLEDPTGYAK RINRMIKLGL
     SLDEEEEAAE ATVVETAPAE VTVGTSSMEQ VD