HSP82_ENCCU
ID HSP82_ENCCU Reviewed; 690 AA.
AC Q8SSE8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Heat shock protein 90;
GN Name=HSP90; OrderedLocusNames=ECU02_1100;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC in cell cycle control and signal transduction. Undergoes a functional
CC cycle that is linked to its ATPase activity. The nucleotide-free form
CC of the dimer is found in an open conformation in which the N-termini
CC are not dimerized and the complex is ready for client protein binding.
CC Binding of ATP induces large conformational changes, resulting in the
CC formation of a ring-like closed structure in which the N-terminal
CC domains associate intramolecularly with the middle domain and also
CC dimerize with each other, stimulating their intrinsic ATPase activity
CC and acting as a clamp on the substrate. Finally, ATP hydrolysis results
CC in the release of the substrate. This cycle probably induces
CC conformational changes in the client proteins, thereby causing their
CC activation. Interacts dynamically with various co-chaperones that
CC modulate its substrate recognition, ATPase cycle and chaperone
CC function. Required for growth at high temperatures (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
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; AL590442; CAD25139.1; -; Genomic_DNA.
DR RefSeq; NP_584635.1; NM_001040824.1.
DR AlphaFoldDB; Q8SSE8; -.
DR SMR; Q8SSE8; -.
DR STRING; 284813.Q8SSE8; -.
DR GeneID; 858625; -.
DR KEGG; ecu:ECU02_1100; -.
DR VEuPathDB; MicrosporidiaDB:ECU02_1100; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q8SSE8; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000000819; Chromosome II.
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; IPR036890; HATPase_C_sf.
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; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..690
FT /note="Heat shock protein 90"
FT /id="PRO_0000383097"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 686..690
FT /note="TPR repeat-binding"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 690 AA; 79082 MW; 9EEA82D024481E16 CRC64;
MSSNQEPLVE GKIKDKHSET HGFEVDVNQM MDTMIKSVYS SKELFLRELV SNSSDACDKL
KALYFQLREK GCVLDPVTSL GIEIIPNKDN RTLTIKDNGI GMTKPDLMNF IGTIASSGTK
KFREEMKEKG NSADASNLIG QFGLGFYSSY LVAERVDLIT KHPSDEALVW TSTGRDVYTI
EEYDGEPFAH GTSLVLYIKE GEEEFLDPKR ISEIVKKYSL FVFYPIYTYV EKEIEEPEEK
KDEEKEDEKV EEETAEPRVE EVREKRLKKV TEREQINVEK PLWKRNIKEV PEEELKSFYK
TVSGDWDDFL AVDFWHIEGL LSIELLMFIP KRARFDMFNK NKKNNNIKLY CKNVFVTDDF
GDAIPEWMSF VSGVVASDDI PMNISREMIQ GTNVMKLVKK TLPQKIFEMI GKLALDAEKY
KTFYKEFGNC LKMAIGEASE GQQDGYAKCL RYFTTKSGEE AISLDTYVER MAPNQKQIYV
ITGLSKEQVK SNPALDAFQK YEVIYMHEVM DEVMLRGLKK YKGHTIQRIT SEGVELPEDE
ASNEEVVKSF EEFCKKVKDI LSSKVEKVTV NPRLVSVPAV ISTTKYSLSG TMENIMKSQP
VTEANPFAAM TAVSKKIFEM NPNHQLVKNL KALFDSNEIE KMNRILEVFF ETVLIHNGFV
LSDPKGFCAN VFDFLCSEEV RCEEPVEEVQ
