ID   DNAK_CYAM1              Reviewed;         607 AA.
AC   Q85FW4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Chaperone protein dnaK;
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332};
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(2003).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; AB002583; BAC76230.1; -; Genomic_DNA.
DR   RefSeq; NP_849068.1; NC_004799.1.
DR   AlphaFoldDB; Q85FW4; -.
DR   SMR; Q85FW4; -.
DR   STRING; 45157.CMV163CT; -.
DR   PRIDE; Q85FW4; -.
DR   EnsemblPlants; CMV163CT; CMV163CT; CMV163C.
DR   GeneID; 844886; -.
DR   Gramene; CMV163CT; CMV163CT; CMV163C.
DR   KEGG; cme:CymeCp136; -.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_4_1; -.
DR   Proteomes; UP000007014; Chloroplast.
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   Reference proteome.
FT   CHAIN           1..607
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078606"
FT   REGION          579..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..607
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  66145 MW;  D81A6423E0054B4C CRC64;
     MAKVVGIDLG TTNSVIAVME GGQPTVVPNS EGFRTTPSVV AYTKNGDLLV GQIAKRQAVI
     NPGNTFYSVK RFIGRKFSEI EQEAKQVPYP VQADGKGNVR IFCSAKDKFF APEEISAQVL
     RKLVDSASQY LGEKVTQAVI TVPAYFNDSQ RQATKDAGKI AGLDVLRIIN EPTAASLAYG
     LDKKSNEKIL VFDLGGGTFD VSILEIGDGV FEVLATSGDT HLGGDDFDKK IVDWLIDNWK
     RIEGIDLSKD KQALQRLTEA AEKAKIELSN VTQTDINLPF ITATADGPKH LDQTLTRAQF
     EQLTSDLIER CRKPVEQALT DAKLSKQDID EVVLVGGSTR IPAVQQLVKD LLGKQPNQSV
     NPDEVVAIGA AIQAGVLAGE VKNILLLDVC PLSLGVETLG GIMTKMIPRN TTIPTRKTEI
     YSTAVDNQTN VEIHVLQGER ELAKDNKSLG TFRLDGIPPA PRGVPQIEVT FDIDANGILS
     VTAKERSTGK QQSITITGAS TLDQSEIERM VKEAEKNAEE DRKKREQIET KNLAESVYYQ
     AEKMGLKDNA QELKNAIDQL DYEGMKNLTQ QVQTLIAQKA SETSNAKTNG KASEKEDVID
     ADFKAQE