ID   HSP71_TRYCR             Reviewed;         656 AA.
AC   P20583;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Heat shock 70 kDa protein, mitochondrial;
DE   Flags: Precursor;
GN   Name=MTP70;
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2689873; DOI=10.1128/mcb.9.11.5163-5168.1989;
RA   Engman D.M., Kirchhoff L.V., Donelson J.E.;
RT   "Molecular cloning of mtp70, a mitochondrial member of the hsp70 family.";
RL   Mol. Cell. Biol. 9:5163-5168(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1565130; DOI=10.1016/0166-6851(92)90210-b;
RA   Engman D.M., Fehr S.C., Donelson J.E.;
RT   "Specific functional domains of mitochondrial hsp70s suggested by sequence
RT   comparison of the trypanosome and yeast proteins.";
RL   Mol. Biochem. Parasitol. 51:153-155(1992).
CC   -!- FUNCTION: May participate in eukaryotic mitochondrial DNA replication.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast.
CC       Note=Associated with kinetoplast DNA in the mitochondrion, in the
CC       region where kdna replication occurs.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; M73627; AAA30215.1; -; Genomic_DNA.
DR   PIR; A33483; A33483.
DR   AlphaFoldDB; P20583; -.
DR   SMR; P20583; -.
DR   PRIDE; P20583; -.
DR   VEuPathDB; TriTrypDB:BCY84_01063; -.
DR   VEuPathDB; TriTrypDB:C3747_28g91; -.
DR   VEuPathDB; TriTrypDB:C4B63_18g293; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_1997; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0078960; -.
DR   VEuPathDB; TriTrypDB:TcCL_NonESM02906; -.
DR   VEuPathDB; TriTrypDB:TcCLB.507029.30; -.
DR   VEuPathDB; TriTrypDB:TcCLB.511211.170; -.
DR   VEuPathDB; TriTrypDB:TCDM_08367; -.
DR   VEuPathDB; TriTrypDB:TcG_13099; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_003281; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0097560; -.
DR   GO; GO:0020023; C:kinetoplast; 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   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Kinetoplast; Mitochondrion;
KW   Nucleotide-binding; Stress response; Transit peptide.
FT   TRANSIT         1..?23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?24..656
FT                   /note="Heat shock 70 kDa protein, mitochondrial"
FT                   /id="PRO_0000013545"
FT   REGION          624..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  71147 MW;  51FF143F5972ECC4 CRC64;
     MFARRLRGAG SLAAASLARW QSSKVTGDVI GIDLGTTYSC VAVMEGDKPR VLENTEGFRA
     TPSVVAFKGQ EKLVGLAAKR QAVTNPQSTF FAVKRLIGRR FEDSNIQHDI KNVPYKIGRS
     SNGDAWVQDA NGKQYSPSQV GAFVLEKMKE TAENFLGRKV SNAVVTCPAY FNGPQRQATK
     DAGTIAGLNV IRVVNGPTAA ALAYGLDKTK DSMIAVYDLG GGTFDISVLE IAGGVFEVKA
     TNGDTHLGGE DFDLCLSDYI LTEFKKSTGI DLSNERMALQ RIREAAEKAK CELSTTMETE
     VNLPFITANQ DGAQHVQMTV SRSKFESLAE KLVQRSLGPC KQCIKDAAVD LKEISEVVLV
     GGMTRMPKVI EAVKQFFGRD PFRGVNPDEA VALGGATLGG VLRRDVKGLV LLDVTPLSLG
     VETLGGVFTR MIPKNTTIPT KKSQTFFSTA AFNQTQVGIK VFQGEREMAA DNQMMGQFDL
     VGIPPAPRGV PQIEVTFDIE PNGICHVTAK DKATGKTQNI TITASGGLSK EQIERMIRDS
     ESHAESDRLK RELVEVRNNA ETQANTAERQ LTEWKYVSDA EKENVRTLLR ACRKSMENPN
     VTKDELSAAT DKLQKAVMEC GRTEYQQAAA GNSSSSSGNT DSSQGEQQQQ GDQQKQ