HSP7M_PHAVU
ID HSP7M_PHAVU Reviewed; 675 AA.
AC Q01899;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Heat shock 70 kDa protein, mitochondrial;
DE Flags: Precursor;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8401600; DOI=10.1046/j.1365-313x.1993.t01-6-00999.x;
RA Vidal V., Ranty B., Dillenschneider M., Charpenteau M., Ranjeva R.;
RT "Molecular characterization of a 70 kDa heat-shock protein of bean
RT mitochondria.";
RL Plant J. 3:143-150(1993).
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; X66874; CAA47345.1; -; mRNA.
DR PIR; S25005; S25005.
DR AlphaFoldDB; Q01899; -.
DR SMR; Q01899; -.
DR STRING; 3885.XP_007148331.1; -.
DR PRIDE; Q01899; -.
DR ProMEX; Q01899; -.
DR eggNOG; KOG0102; Eukaryota.
DR PhylomeDB; Q01899; -.
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; 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; Stress response;
KW Transit peptide.
FT TRANSIT 1..51
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 52..675
FT /note="Heat shock 70 kDa protein, mitochondrial"
FT /id="PRO_0000013548"
FT REGION 638..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 72537 MW; 7A85763879CC8272 CRC64;
MAAVLRSLRR RDVASATFSA YRSLTGSTKP AYVAQKWSCL ARPFSSRPAG NDVIGIDLGT
TNSCVSVMEG KNPKVIENSE GARTTPSVVA FNQKGELLVG TPAKRQAVTN PTNTVFGTKR
LIGRRFDDPQ TQKEMKMVPF KIVKAPNGDA WVEANGQQYS PSQIGAFVLT KMKETAEAYL
GKSVSKAVIT VPAYFNDAQR QATKDAGRIA GLDVQRIINE PTAAALSYGM NNKEGLIAVF
DLGGGTFDVS ILEISNGVFE VKATNGDTFL GGEDFDNALL DFLVNEFKRT ESIDLSKDRL
ALQRLREAAE KAKIELSSTS QTEINLPFIT ADASGAKHLN ITLTRSKFEA LVNHLIERTK
APCKSCLKDA NVSIKDVDEV LLVGGMTRVP KVQEVVLNIF GKSPSKGVNP DEAVAMGAAI
QGGILRGDVK ELLLLDVTPL SLGIETLGGI FTRLINRNTT IPTKKSQVFS TAADNQTQVG
IKVLQGEREM ASDNKMLGEF DLVGIPPAPR GLPQIEVTFD IDANGIVTVS AKDKSTGKEQ
QITIRSSGGL SEDEIEKMVK EAELHAQKDQ ERKTLIDIRN SADTTIYSIE KSLGEYREKI
PSETAKEIED AVSDLRKAMS GDNVDEIKSK LDAANKAVSK IGEHMSGGSS GGSSAGGSQG
GGDQAPEAEY EEVKK
