HSP83_TRYBB
ID HSP83_TRYBB Reviewed; 703 AA.
AC P12861;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Heat shock protein 83;
GN Name=HSP83;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LstaR;
RX PubMed=2515434; DOI=10.1016/0166-6851(89)90108-4;
RA Mottram J., Murphy W., Agabian N.;
RT "A transcriptional analysis of the Trypanosoma brucei hsp83 gene cluster.";
RL Mol. Biochem. Parasitol. 37:115-128(1989).
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.
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; X14176; CAA32377.1; -; Genomic_DNA.
DR PIR; S08119; S08119.
DR PDB; 3OPD; X-ray; 2.60 A; A/B/C=1-213.
DR PDBsum; 3OPD; -.
DR AlphaFoldDB; P12861; -.
DR SMR; P12861; -.
DR PRIDE; P12861; -.
DR EvolutionaryTrace; P12861; -.
DR GO; GO:0005813; C:centrosome; ISA:GeneDB.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; ISA:GeneDB.
DR GO; GO:0042026; P:protein refolding; ISA:GeneDB.
DR GO; GO:0009408; P:response to heat; NAS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; ISA:GeneDB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Stress response.
FT CHAIN 1..703
FT /note="Heat shock protein 83"
FT /id="PRO_0000062944"
FT REGION 211..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 699..703
FT /note="TPR repeat-binding"
FT COMPBIAS 213..227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Polar 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 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 29..50
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3OPD"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3OPD"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:3OPD"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:3OPD"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3OPD"
SQ SEQUENCE 703 AA; 80716 MW; 50D7BB333A303B70 CRC64;
MTETFAFQAE INQLMSLIIN TFYSNKEIFL RELISNSSDA CDKIRYQSLT NQSVLGDEPH
LRIRVIPDRV NKTLTVEDSG IGMTKADLVN NLGTIARSGT KSFMEALEAG GDMSMIGQFG
VGFYSAYLVA DRVTVVSKNN EDDAYTWESS AGGTFTVTST PDCDLKRGTR IVLHLKEDQQ
EYLEERRLKD LIKKHSEFIG YDIELMVENT TEKEVTDEDE DEEAAKKAEE GEEPKVEEVK
DGVDADAKKK KTKKVKEVKQ EFVVQNKHKP LWTRDPKDVT KEEYASFYKA ISNDWEEQLS
TKHFSVEGQL EFRAILFLPK RAPFDMFEPN KKRNNIKLYV RRVFIMDNCE DLCPEWLGFL
RGVVDSEDLP LNISRENLQQ NKILKVIRKN IVKKALELFE ELAGNKEDYK KFYEQFSKNV
KLGIHEDSTN RKKLMELLRF HSSESGEEMT TLKDYVTRMK EGQKCIYYVT GDSKKKLETS
PFIEQARRRG MEVLFMTDPI DEYVMQQVKD FEDKKFACLT KEGVHFEETE EEKKQREEEK
ASYERLCKAM KEVLGDKVEK VVVSDRLATS PCILVTSEFG WSAHMEQIMR NQALRDSSMS
AYMMRKKTME INTTHAIVKE LKRRVEADEN DKAAKDLIFL LFDTSLLTSG FTLDDPTAYA
DRIHRMIKLG LSLDDDAEEE EAQAPVAAAA NSSTGASGME EVD
