ID   HSP71_LEIMA             Reviewed;         634 AA.
AC   P12076;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Heat shock 70-related protein 1, mitochondrial;
DE   Flags: Precursor;
GN   Name=HSP70.1;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=8314893; DOI=10.1242/jcs.104.4.1091;
RA   Searle S., McCrossan M.V., Smith D.F.;
RT   "Expression of a mitochondrial stress protein in the protozoan parasite
RT   Leishmania major.";
RL   J. Cell Sci. 104:1091-1100(1993).
RN   [2]
RP   SEQUENCE REVISION TO 461-500.
RA   Smith D.F.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-249.
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=2762121; DOI=10.1093/nar/17.13.5081;
RA   Searle S., Campos A.J.R., Coulson R.M.R., Spithill T.W., Smith D.F.;
RT   "A family of heat shock protein 70-related genes are expressed in the
RT   promastigotes of Leishmania major.";
RL   Nucleic Acids Res. 17:5081-5095(1989).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; X64137; CAA45498.2; -; Genomic_DNA.
DR   EMBL; X14574; CAA32713.1; -; Genomic_DNA.
DR   PIR; S33575; S33575.
DR   AlphaFoldDB; P12076; -.
DR   SMR; P12076; -.
DR   STRING; 5664.LmjF.30.2460; -.
DR   PRIDE; P12076; -.
DR   VEuPathDB; TriTrypDB:LmjF.30.2460; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_300032000; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_300031900; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
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; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Mitochondrion; Nucleotide-binding;
KW   Stress response; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..634
FT                   /note="Heat shock 70-related protein 1, mitochondrial"
FT                   /id="PRO_0000013544"
FT   COILED          538..614
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   634 AA;  68330 MW;  8382B1C40C108EEA CRC64;
     MFARRVCGSA AASAACLARH ESQKVQGDVI GVDLGTTYSC VATMDGDKAR VLENSEGFRT
     TPSVVAFKGS EKLVGLAAKR QAITNPQSTF YAVKRLIGRR FEDEHIQKDI KNVPYKIVRA
     GNGDAWVQDG NGKQYSPSQI GAFVLEKMKE TAENFLGHKV SNAVVTCPAY FNDAQRQATK
     DAGTIAGLNV IRVVNEPTAA ALAYGMDKTK DSLIAVYDLG GGTFDISVLE IAGGVFEVKA
     TNGDTHLGGE DFDLALSDYI LEEFRKTSGI DLSKERMALQ RVREAAEKAK CELSSAMETE
     VNLPFITANA DGAQHIQMRI SRSKFEGITQ RLIERSIAPC KQCMKDAGVE LKEINDVVLV
     GGMTRIRSGG GGEEVLPEGP VRGVNPDEAV ALGAATLGGV LRGKASDLIL VDVTPLSLGT
     SVVGDVFVPI IPKNTTIPCM RSHIFTTVDD GQTAIKFKVF QGEREIASEN QIRGEFDLSG
     IPPAPRGVPQ VEVTFDIDAN GICHVTAKDK ATGKTQNITI TANGGLSKEQ IEQMIRDSEQ
     HAEADRVKRE LVEVRNNAET QLTTAERQLG EWKYVSDAEK ENVKTLVAEL RKAMENPNVA
     KDDLAAATDK LQKAVMECGR TEYQQAAAAN SGQC