ID   HSP7M_SOLTU             Reviewed;         682 AA.
AC   Q08276;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Heat shock 70 kDa protein, mitochondrial;
DE   Flags: Precursor;
GN   Name=HSP68;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7763614; DOI=10.1007/bf00195672;
RA   Neumann D., Emmermann M., Thierfelder J.M., zur Nieden U., Clericus M.,
RA   Braun H.P., Nover L., Schmitz U.K.;
RT   "HSP68 -- a DnaK-like heat-stress protein of plant mitochondria.";
RL   Planta 190:32-43(1993).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; S59747; AAC60559.2; -; mRNA.
DR   PIR; T07024; T07024.
DR   RefSeq; NP_001305489.1; NM_001318560.1.
DR   AlphaFoldDB; Q08276; -.
DR   SMR; Q08276; -.
DR   IntAct; Q08276; 1.
DR   STRING; 4113.PGSC0003DMT400027703; -.
DR   PRIDE; Q08276; -.
DR   ProMEX; Q08276; -.
DR   GeneID; 102582209; -.
DR   KEGG; sot:102582209; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   InParanoid; Q08276; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q08276; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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; SSF100934; SSF100934; 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   2: Evidence at transcript level;
KW   ATP-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Stress response; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           58..682
FT                   /note="Heat shock 70 kDa protein, mitochondrial"
FT                   /id="PRO_0000013549"
FT   REGION          649..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  73077 MW;  F4F2ADE7C030F7B6 CRC64;
     MATAALLRSL RRREFATSSI SAYRTLASNT KPSWCPSLVG AKWAGLARPF SSKPAGNEII
     GIDLGTTNSC VAVMEGKNPK VIENSEGART TPSVVAFNQK GELLVGTPAK RQAVTNPTNT
     LSGTKRLIGR RFDDPQTQKE MKMVPYKIVR GSNGDAWVEA NGQQYSPTQI GAFILTKMKE
     TAEAYLGKSI NKAVITVPAY FNDAQRQAIK DAGAIAGLDV QRIINEPTAA ALSYGMNSKE
     GLVAVFDLGG GTFDVSILEI SNGVFEVKAT NGDTFLGGED FDNALLEFLV SEFKRTEGID
     LSKDKLALQR LREAAEKAKI ELSSTSQTDI NLPFITADAS GAKHLNITLT RSKFETLVNH
     LIERTRNPCK NCLKDAGVSL KDVDEVLLVG GMTRVPKVQE IVSEIFGKSP SKGVNPDEAV
     AMGAALQGGI LRGDVKELLL LDVTPLARGI ETLGGIFTRL INRNTTIPTK KSQVFSTAAD
     NQTQVGIKVL QGEREMASDN KLLGEFDLVG IPPAPKGYCP QIEVIFDIDA NGMVTVSAKD
     KATSKEQQIT IRSSGGLSED EIDKMVREAE MHAQRIKNAR HLLISGIVQS TTIYSIEKSL
     SEYKEKVPKE VVTEIETAIS DLRAAMGTEN IDDIKAKLDA ANKAVSKIGE HMAGGSSGGA
     SGGGGAQGGD QPPEAEYEEV KK