HSP72_DROSI
ID HSP72_DROSI Reviewed; 643 AA.
AC Q9GSU4; Q9GNI6; Q9GSU5; Q9GSU6;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Major heat shock 70 kDa protein Ba;
DE Short=Heat shock protein 70Ba;
DE AltName: Full=HSP70-87C1;
GN Name=Hsp70Ba;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240 {ECO:0000312|EMBL:AAG24845.1};
RN [1] {ECO:0000312|EMBL:AAG24845.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSR 1 {ECO:0000312|EMBL:AAG24842.1},
RC DSR 2 {ECO:0000312|EMBL:AAG24843.1}, DSR 3 {ECO:0000312|EMBL:AAG24844.1},
RC and DSR 4 {ECO:0000312|EMBL:AAG24845.1};
RX PubMed=11965431; DOI=10.1007/s00239-001-0044-7;
RA Bettencourt B.R., Feder M.E.;
RT "Rapid concerted evolution via gene conversion at the Drosophila hsp70
RT genes.";
RL J. Mol. Evol. 54:569-586(2002).
CC -!- INDUCTION: Heat shock induces the synthesis of seven proteins at five
CC otherwise inactive sites in the polytene chromosomes of fruit fly
CC larvae. Two separate sites, producing two and three copies,
CC respectively, code for the 70 kDa protein. {ECO:0000305}.
CC -!- MISCELLANEOUS: Most strains have three copies of the gene coding for
CC this protein at chromosome locus 87C1; two tandemly repeated Hsp70
CC genes (Hsp70Bb and Hsp70Bc) and one in reverse orientation (Hsp70Ba).
CC Some strains, including that sequenced in the Drosophila genome project
CC have three tandemly repeated Hsp70 genes (Hsp70Bb, Hsp70Bbb and
CC Hsp70Bc). {ECO:0000250|UniProtKB:P02824}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|RuleBase:RU003322, ECO:0000305}.
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DR EMBL; AF295971; AAG24842.1; -; Genomic_DNA.
DR EMBL; AF295972; AAG24843.1; -; Genomic_DNA.
DR EMBL; AF295973; AAG24844.1; -; Genomic_DNA.
DR EMBL; AF295974; AAG24845.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GSU4; -.
DR SMR; Q9GSU4; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Stress response.
FT CHAIN 1..643
FT /note="Major heat shock 70 kDa protein Ba"
FT /id="PRO_0000078336"
FT REGION 611..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 25
FT /note="I -> T (in strain: DSR 2)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 208
FT /note="T -> A (in strain: DSR 1)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 286
FT /note="F -> L (in strain: DSR 3)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 306
FT /note="D -> N (in strain: DSR 4)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 358
FT /note="N -> S (in strain: DSR 1)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 483
FT /note="I -> T (in strain: DSR 2)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 617
FT /note="A -> T (in strain: DSR 3)"
FT /evidence="ECO:0000269|PubMed:11965431"
SQ SEQUENCE 643 AA; 70303 MW; 29237D6AB8C96C16 CRC64;
MPAIGIDLGT TYSCVGVYQH GKVEIIANDQ GNRTTPSYVA FTDSERLIGD PAKNQVAMNP
RNTVFDAKRL IGRKYDDPKI AEDMKHWPFK VVSDCGKPKI GVEYKGESKR FAPEEISSMV
LAKMKETAEA YLGESITDAV ITVPAYFNDS QRQATKDAGH IAGLNVLRII NEPTAAALAY
GLDKNLKGER NVLIFDLGGG TFDVSILTID EGSLFEVRST AGDTHLGGED FDNRLVTHLA
EEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEATI EIDALFEGQD FYTKVSRARF
EELCADLFRN TLQPVEKALT DAKMDKGQIH DIVLVGGSTR IPKVQSLLQE FFHGKNLNLS
INPDEAVAYG AAVQAAILSG DQSGKIQDVL LVDVAPLSLG IETAGGVMTK LIERNCRIPC
KQTKTFSTYS DNQPGVSIQV YEGERAMTKD NNALGTFDLS GIPPAPRGVP QIEVTFDLDA
NGILNVSAKE MSTGKAKNIT IKNDKGRLSQ AEIDRMVNEA EKYADEDEKQ RQRITSRNAL
ESYVFNVKQS VEQAPAGKLD EADKNSVLDK CNDTIRWLDS NTTAEKEEFD HKMEELTRHC
SPIMTKMHQQ GAGAGAAGGP GANCGQQAGG FGGYSGPTVE EVD