ID   HSP7M_PEA               Reviewed;         675 AA.
AC   P37900;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Heat shock 70 kDa protein, mitochondrial;
DE   Flags: Precursor;
GN   Name=HSP1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1731975; DOI=10.1007/bf00018453;
RA   Watts F.Z., Walters A.J., Moore A.L.;
RT   "Characterisation of PHSP1, a cDNA encoding a mitochondrial HSP70 from
RT   Pisum sativum.";
RL   Plant Mol. Biol. 18:23-32(1992).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; X54739; CAA38536.1; -; mRNA.
DR   PIR; S19140; S19140.
DR   AlphaFoldDB; P37900; -.
DR   SMR; P37900; -.
DR   IntAct; P37900; 2.
DR   MINT; P37900; -.
DR   PRIDE; P37900; -.
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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Mitochondrion; Nucleotide-binding; Stress response;
KW   Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           53..675
FT                   /note="Heat shock 70 kDa protein, mitochondrial"
FT                   /id="PRO_0000013547"
FT   REGION          639..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  72301 MW;  56DCDFF6F4C97E5B CRC64;
     MAATLLRSLQ RRNLSSSSVS AFRSLTGSTK TSYATHKLAS LTRPFSSRPA GNDVIGIDLG
     TTNSCVSVME GKNPKVIENS EGARTTPSVV AFNQKSELLV GTPAKRQAVT NPTNTLFGTK
     RLIGRRFDDA QTQKEMKMVP YKIVRAPNGD AWVEANGQQY SPSQIGAFVL TKIKETAEAY
     LGKTISKAVV TVPAYFNDAQ RQATKDAGRI AGLDVQRIIN EPTAAALSYG MNNKEGLIAV
     FDLGGGTFDV SILEISNGVF EVKATNGDTF LGGEDFDNAL LDFLVSEFKR TESIDLAKDK
     LALQRLREAA EKAKIELSST SQTEINLPFI SADASGAKHL NITLTRSKFE ALVNNLIERT
     KAPCKSCLKD ANISIKDVDE VLLVGGMTRV PKVQQVVSEI FGKSPSKGVN PDEAVAMGAA
     LQGGILRGDV KELLLLDVTP LSLGIETLGG IFTRLISRNT TIPTKKSQVF STAADNQTQV
     GIKVLQGERE MAADNKSLGE FDLVGIPPAP RGLPQIEVTF DIDANGIVTV SAKDKSTGKE
     QQITIRSSGG LSDDEIDKMV KEAELHAQRD QERKALIDIR NSADTSIYSI EKSLAEYREK
     IPAEVAKEIE DAVSDLRTAM AGENADDIKA KLDAANKAVS KIGQHMSGGS SGGPSEGGSQ
     GGEQAPEAEY EEVKK