ID O50047_SPIOL Unreviewed; 675 AA.
AC O50047;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Heat shock 70 kDa protein, mitochondrial-like {ECO:0000313|RefSeq:XP_021859966.1};
DE SubName: Full=Heat shock 70 protein {ECO:0000313|EMBL:AAB96660.1};
GN Name=HSC70-11 {ECO:0000313|EMBL:AAB96660.1};
GN Synonyms=LOC110799072 {ECO:0000313|RefSeq:XP_021859966.1};
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562 {ECO:0000313|EMBL:AAB96660.1};
RN [1] {ECO:0000313|EMBL:AAB96660.1}
RP NUCLEOTIDE SEQUENCE.
RA Li Q.B., Guy C.L.;
RT "The organization and evolution of the spinach stress 70 molecular
RT chaperones.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAB91473.1, ECO:0000313|RefSeq:XP_021859966.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bloomsdale {ECO:0000313|EMBL:AAB91473.1};
RX PubMed=10080706; DOI=10.1023/A:1006100532501;
RA Li Q.B., Haskell D.W., Guy C.L.;
RT "Coordinate and non-coordinate expression of the stress 70 family and other
RT molecular chaperones at high and low temperature in spinach and tomato.";
RL Plant Mol. Biol. 39:21-34(1999).
RN [3] {ECO:0000313|Proteomes:UP001155700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Sp75 {ECO:0000313|Proteomes:UP001155700};
RX PubMed=28537264; DOI=10.1038/ncomms15275;
RA Xu C., Jiao C., Sun H., Cai X., Wang X., Ge C., Zheng Y., Liu W., Sun X.,
RA Xu Y., Deng J., Zhang Z., Huang S., Dai S., Mou B., Wang Q., Fei Z.,
RA Wang Q.;
RT "Draft genome of spinach and transcriptome diversity of 120 Spinacia
RT accessions.";
RL Nat. Commun. 8:15275-15275(2017).
RN [4] {ECO:0000313|RefSeq:XP_021859966.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; AF035458; AAB91473.1; -; mRNA.
DR EMBL; AF039084; AAB96660.1; -; Genomic_DNA.
DR PIR; T08901; T08901.
DR RefSeq; XP_021859966.1; XM_022004274.1.
DR IntAct; O50047; 1.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP001155700; Unplaced.
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 CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP001155700};
KW Stress response {ECO:0000313|EMBL:AAB96660.1,
KW ECO:0000313|RefSeq:XP_021859966.1}.
FT REGION 636..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..325
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 675 AA; 72371 MW; F700DF0C1C859FBD CRC64;
MATALRRCLR PEQFRSFPAF KSLAGNASPS LSSPYMAQRL ASLVRPFSSR PAGNDVIGID
LGTTNSCVSV MEGKSAKVIE NAEGARTTPS VVAFNPKGEL LVGTPAKRQA VTNPTNTIFG
TKRLIGRVFS DPQTQKEMKM VPYKIVKAPN GDAWVEANGQ QYSPSQVGAF VLTKMKETAE
AYLGKTVSKA VVTVPAYFND AQRQATKDAG KIAGLDVQRI INEPTAAALS YGMTNKEGLI
AVFDLGGGTF DVSILEISNG VFEVKATNGD TFLGGEDFDN TLLEFLVSEF KKTEGIDLSS
DRLALQRLRE AAEKAKIELS STSQTDISLP FISADSSGAK HLNITLSRSK FESLVGNLIE
RTRAPCKNCL KDAGVSLNEV DEVLLVGGMT RVPKVQEIVQ EIFGKSPSKG VNPDEAVAMG
AAIQGGILRG DVKDLLLLDV TPLSLGIETL GGVFTRLINR NTTIPTKKSQ VFSTAADNQT
QVGIKVLQGE REMASDNKML GEFELQGIPP APRGLPQIEV TFDIDANGIV TVSAKDKATN
KEQNITIKSS GGLSEHEIEK MVKEAEIHAQ KDQERKSLID ARNTADTTIY SVEKSLGEYR
EKIPTEIAKE IEDAVSDLRS AMQNDNLEEI KAKTDAANKA VSKIGEHMSG GQGGGSSSSG
GADQTPEAEY EEAKK
//
