ID   DNAK_CYACA              Reviewed;         618 AA.
AC   Q9TLT1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
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;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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; AF022186; AAF12906.1; -; Genomic_DNA.
DR   RefSeq; NP_045188.1; NC_001840.1.
DR   AlphaFoldDB; Q9TLT1; -.
DR   SMR; Q9TLT1; -.
DR   GeneID; 800254; -.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Stress response.
FT   CHAIN           1..618
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078605"
SQ   SEQUENCE   618 AA;  68192 MW;  F23DEFC895699006 CRC64;
     MEKIVGIDLG TTNSVIAVME MGKPAVIPNS EGFRTTPSVV AYAKNGDLLV GQIAKRQAVI
     NPSNTFYSVK RFIGRKFEEI NEENRQVTYQ VNKDPSGNVK IYCPFKNKDF TPEEISAQVI
     RKLTEGASKY LGEKITKAVI TVPAYFNDSQ RQATKDAGKI AGLDVLRIIN EPTAASLAYG
     LDKKNNEKIL VFDLGGGTFD VTILEIGDGI FEVLSTSGDT HLGGDDFDKK IVDWLVDEFK
     KSYNIDLSKD KQALQRLTEA AEKAKIELSS VSQTEINLPF ITATSEGPIH FDKSLNRAKF
     EELVSELIAR CKIPVENALK DAKLNKSDIN EIVLVGGSTR IPAIQNLVKE SLQKDPNQTV
     NPDEVVAVGA AIQGAVLAGE VKDILLLDVC PLSLGVETLG GVMTKMIPKN TTIPTRKTEI
     YSTAVDNQTN VEIHVLQGER ELAKDNKSLG TFRLDGIPPA PRGVPQIEVT FDIDANGILS
     VTAKEKTTGK QQSVTITGAS TLDKDEIQKI IKEAEINAQE DRKKKENIEL KNQAETICYQ
     AQKQLNEFKE KIDKNQYKRI EDLIAKLKQA ISSNEYEEIK NLMEAIQKET MEIGKELYSK
     DSKNTKNSDV IDADFSET