ID   HSP83_DROPB             Reviewed;         269 AA.
AC   O16068; O16069; O16070; O16071; O16072; O16073; O16074; O16075; O61306;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Heat shock protein 83;
DE   AltName: Full=HSP 82;
DE   Flags: Fragment;
GN   Name=Hsp83; Synonyms=Hsp82;
OS   Drosophila pseudoobscura bogotana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-79.
RC   STRAIN=Bogota60, Bogota61, Bogota62, Bogota63, Bogota67, Bogota70,
RC   Bogota73, Bogota74, and Bogota77;
RX   PubMed=9383055; DOI=10.1093/genetics/147.3.1091;
RA   Wang R.L., Wakeley J., Hey J.;
RT   "Gene flow and natural selection in the origin of Drosophila pseudoobscura
RT   and close relatives.";
RL   Genetics 147:1091-1106(1997).
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. Required for piRNA biogenesis by facilitating
CC       loading of piRNAs into PIWI proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with shu (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; AF006540; AAC07925.1; -; Genomic_DNA.
DR   EMBL; AF006541; AAC07926.1; -; Genomic_DNA.
DR   EMBL; AF006542; AAC07927.1; -; Genomic_DNA.
DR   EMBL; AF006543; AAC07928.1; -; Genomic_DNA.
DR   EMBL; AF006544; AAC07929.1; -; Genomic_DNA.
DR   EMBL; AF006545; AAC07930.1; -; Genomic_DNA.
DR   EMBL; AF006546; AAC07931.1; -; Genomic_DNA.
DR   EMBL; AF006547; AAC07932.1; -; Genomic_DNA.
DR   EMBL; AF006548; AAC07933.1; -; Genomic_DNA.
DR   PRIDE; O16068; -.
DR   FlyBase; FBgn0021235; Dpsb\Hsp83.
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; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 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..>269
FT                   /note="Heat shock protein 83"
FT                   /id="PRO_0000062932"
FT   REGION          206..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   VARIANT         79
FT                   /note="I -> V (in strain: Bogota70)"
FT                   /evidence="ECO:0000269|PubMed:9383055"
FT   NON_TER         269
SQ   SEQUENCE   269 AA;  30117 MW;  40F942117B67CAAC CRC64;
     MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYX SXTDPXKLXX
     XXXXXXXXIP NKTAGTLTII DTGIXMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
     QFGVGFYSAY LIADRVTVTS KNNDDEQYVW ESSAGGSFTV KADNSEPLGR GTKIXLYIKE
     DQTDYLEESK IKEIVNKHSQ FIGYPXKXXX EKERXKEVSD DEADDEKKDD EAKKDMDTDE
     PKIEDVGEDE DADKKDKDGK KKKTIKEKY