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 08-NOV-2023, entry version 89.
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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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
//
