HSOP_PLAFA
ID HSOP_PLAFA Reviewed; 252 AA.
AC P25407;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Hsp70-Hsp90 organising protein {ECO:0000250|UniProtKB:Q8ILC1};
DE Short=PfHOP {ECO:0000250|UniProtKB:Q8ILC1};
DE AltName: Full=Stress-inducible protein 1 {ECO:0000250|UniProtKB:Q8ILC1};
DE Flags: Fragment;
GN Name=HOP {ECO:0000250|UniProtKB:Q8ILC1};
GN Synonyms=STI1 {ECO:0000250|UniProtKB:Q8ILC1};
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T9/96 / Thailand;
RX PubMed=1852174; DOI=10.1016/0166-6851(91)90195-c;
RA Robson K.J.H., Jennings M.W.;
RT "The structure of the calmodulin gene of Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 46:19-34(1991).
CC -!- FUNCTION: Acts as a co-chaperone and mediates the association of the
CC chaperones HSP70 and HSP90 probably facilitating substrate transfer
CC from HSP70 to HSP90. Stimulates HSP70 ATPase activity and, in contrast,
CC inhibits HSP90 ATPase activity. {ECO:0000250|UniProtKB:Q8ILC1}.
CC -!- SUBUNIT: Monomer. Homodimer. Forms a complex composed of HOP and
CC chaperones HSP70 and HSP90; the interaction is stronger in the absence
CC of ATP. Interacts (via TPR 1, 2, 3, 7, 8 and 9 repeats) with HSP70 (via
CC C-terminus); the interaction is direct and is stronger in the absence
CC of ATP. Interacts (via TPR 4, 5 and 6 repeats) with HSP90 (via C-
CC terminus); the interaction is direct. {ECO:0000250|UniProtKB:Q8ILC1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8ILC1}.
CC -!- DOMAIN: The TPR repeats form 3 domains; the TPR 1 domain is composed of
CC TPR 1, 2 and 3 repeats, the TPR2A domain of TPR 4, 5 and 6 repeats and
CC TPR2B domain of TPR 7, 8 and 9 repeats. {ECO:0000250|UniProtKB:Q8ILC1}.
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DR EMBL; M59770; AAA29511.1; -; Genomic_DNA.
DR PIR; A45594; A45594.
DR AlphaFoldDB; P25407; -.
DR SMR; P25407; -.
DR EnsemblProtists; CZU00040; CZU00040; PF3D7_1434300.
DR VEuPathDB; PlasmoDB:PF3D7_1434300; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000508100; -.
DR VEuPathDB; PlasmoDB:Pf7G8_140039500; -.
DR VEuPathDB; PlasmoDB:PfCD01_140039700; -.
DR VEuPathDB; PlasmoDB:PfDd2_140038700; -.
DR VEuPathDB; PlasmoDB:PfGA01_140039800; -.
DR VEuPathDB; PlasmoDB:PfGB4_140040400; -.
DR VEuPathDB; PlasmoDB:PfGN01_140039600; -.
DR VEuPathDB; PlasmoDB:PfHB3_140040000; -.
DR VEuPathDB; PlasmoDB:PfIT_140040700; -.
DR VEuPathDB; PlasmoDB:PfKE01_140039200; -.
DR VEuPathDB; PlasmoDB:PfKH01_140039800; -.
DR VEuPathDB; PlasmoDB:PfKH02_140040000; -.
DR VEuPathDB; PlasmoDB:PfML01_140039700; -.
DR VEuPathDB; PlasmoDB:PfNF135_140038500; -.
DR VEuPathDB; PlasmoDB:PfNF166_140037200; -.
DR VEuPathDB; PlasmoDB:PfNF54_140038100; -.
DR VEuPathDB; PlasmoDB:PfSD01_140037600; -.
DR VEuPathDB; PlasmoDB:PfSN01_140041500; -.
DR VEuPathDB; PlasmoDB:PfTG01_140039600; -.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR045248; Sti1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Chaperone; Coiled coil; Cytoplasm; Repeat; TPR repeat.
FT CHAIN 1..>252
FT /note="Hsp70-Hsp90 organising protein"
FT /id="PRO_0000066166"
FT REPEAT 7..40
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 41..74
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 75..108
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REGION 199..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..239
FT /evidence="ECO:0000255"
FT NON_TER 252
SQ SEQUENCE 252 AA; 29324 MW; 5283E694BCCDDF3C CRC64;
MVNKEEAQRL KELGNKCFQE GKYEEAVKYF SDAITNDPLD HVLYSNLSGA FASLGRFYEA
LESANKCISI KKDWPKGYIR KGCAEHGLRQ LSNAEKTYLE GLKIDPNNKS LQDALSKVRN
ENMLENAQLI AHLNNIIEND PQLKSYKEEN SNYPHELLNT IKSINSNPMN IRIILSTCHP
KISEGVEKFF GFKFTGEGND AEERQRQQRE EEERRKKKEE EERKKKEEEE MKKQNRTPEQ
IQGDEHKLKV MN
