ID   DNAK_DIALT              Reviewed;         629 AA.
AC   P30722;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Chaperone protein dnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; Synonyms=hsp70;
OS   Diacronema lutheri (Unicellular marine alga) (Monochrysis lutheri).
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Pavlovales; Pavlovaceae; Diacronema.
OX   NCBI_TaxID=2081491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1536924; DOI=10.1007/bf00040663;
RA   Scaramuzzi C.D., Stokes H.W., Hiller R.G.;
RT   "Heat shock Hsp70 protein is chloroplast-encoded in the chromophytic alga
RT   Pavlova lutherii.";
RL   Plant Mol. Biol. 18:467-476(1992).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; X59555; CAA42154.1; -; Genomic_DNA.
DR   PIR; S20516; S20516.
DR   AlphaFoldDB; P30722; -.
DR   SMR; P30722; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; 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; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Stress response.
FT   CHAIN           1..629
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078610"
FT   REGION          599..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  68792 MW;  C388D0C369979D66 CRC64;
     MAKVVGIDLG TTNSVVAVME GGKPTVITNS EGGTTTPSVV AYAKNGDLLV GQIAKRQAVI
     NSENTFYSVK RFIGRPSKEV SDELRQTPYK IEDSEGKIRL KCPNLNKNFA AEEISAQVLR
     KLVNDANKYL GEKVEKAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAASLAYGL
     DKKDNETILV FDLGGGTFDV SILEVGDGVF EVLSTSGDTR LGGDDFDEKI VKWLLNEFEK
     EEKFSLKGDS QALQRLTEAA EKAKIELSSL SQTEINLPFI TANENGAKHI EKTLTGEKFE
     SLCSDLFDRC RIPVENALKD AKLKPNQIDE VVLVGGSTRI PAVKKLVKDI LGKEPNETVN
     PDEVVAIGAA IQAGVLSGEV KDILLLDVTP LSLGVETLGG VTTKIIPRNT TVPTKKSEIF
     STAVDNQPNV EIHVLQGERE FARDNKSLGT FRLDGILPAP RGIPQIEVTF DIDANGILSV
     TAQDKGTSKQ QSITISGAST LPKEEVEKMV KEAEQNAAAD KEKGENIRVK NEADLYCYQA
     EKQISELPEA LVNENQSLIK ESKETVEMLK ENIKKEDYDK IKENLKKLQE KLMEIGQKAY
     AKKEPLKDED SNKAGSQDDF IDADFTESK