ID   HSP83_LEIIN             Reviewed;         701 AA.
AC   Q25293;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Heat shock protein 83-1;
DE            Short=HSP 83;
GN   Name=HSP83-1;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/FR/78/LEM 75;
RX   PubMed=8971277; DOI=10.1016/s0001-706x(96)00020-4;
RA   Angel S.O., Requena J.M., Soto M., Criado D., Alonso C.;
RT   "During canine leishmaniasis a protein belonging to the 83-kDa heat-shock
RT   protein family elicits a strong humoral response.";
RL   Acta Trop. 62:45-56(1996).
RN   [2]
RP   SEQUENCE REVISION TO 654.
RA   Requena J.M.;
RL   Submitted (APR-2002) 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: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; X87770; CAD30506.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q25293; -.
DR   SMR; Q25293; -.
DR   STRING; 5671.XP_003392730.1; -.
DR   VEuPathDB; TriTrypDB:LINF_330009000; -.
DR   VEuPathDB; TriTrypDB:LINF_330009700; -.
DR   eggNOG; KOG0019; Eukaryota.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..701
FT                   /note="Heat shock protein 83-1"
FT                   /id="PRO_0000062941"
FT   REGION          210..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           697..701
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        227..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   701 AA;  80680 MW;  A7FF41FF5264BF08 CRC64;
     MTETFAFQAE INQLMSLIIN TFYSNKEIFL RELISNASDA CDKIRYQSLT DPSVLGESPR
     LCIRVVPDKE NKTLTVEDNG IGMTKADLVN NLGTIARSGT KAFMEALEAG GDMSMIGQFG
     VGFYSAYLVA DRVTVTSKNN SDESYVWESS ACGTFTITST PESDMKRGTR ITLHLKEDQM
     EYLEPRRLKE LIKKHSEFIG YDIELMVEKT TEKEVTDEDE EDTKKADEDE EPKVEEVREG
     DEGEKKKTKK VKEVTKEYEV QNKHKPLWTR DPKDVTKEEY AAFYKAISND WEDPRATKHF
     SVEGQLEFRS IMFVPKRAPF DMFEPNKKRN NIKLYVRRVF IMDNCEDLCP DWLGFVKGVV
     DSEDLPLNIS RENLQQNKIL KVIRKNIVKK CLEMFDEVAE NKEDYKQFYE QFGKNIKLGI
     HQDTANRKKL MEFVRFYSSE SGEEMTTLKD YVTRMKAGQK SIYYITGDSK KKLESSPFIE
     QAKRRGLEVL FMTEPIDEYV MQQVKDFEDK KFACLTKEGV HFEESEEEKQ QREEEKAACE
     KLCKTMKEVL GDKVEKVIVS ECLSTSPCIL VTSEFGWSAH MEQIMRNQAL RDSSMAQYMM
     SKKTMELNPR HPIIKELRRR VDADENDKAV KDLVFLLFDT SLLTSGFQLE DPTGYAERIN
     RMIKLGLSLD EEEEVVAAEA TVAETAPAEV TAGTSSMEQV D