ID   DNAK_THAPS              Reviewed;         602 AA.
AC   A0T0X1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
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   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA   Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA   Green B.R.;
RT   "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT   Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT   lineage.";
RL   Mol. Genet. Genomics 277:427-439(2007).
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; EF067921; ABK20806.1; -; Genomic_DNA.
DR   RefSeq; YP_874583.1; NC_008589.1.
DR   AlphaFoldDB; A0T0X1; -.
DR   SMR; A0T0X1; -.
DR   PRIDE; A0T0X1; -.
DR   GeneID; 4524722; -.
DR   InParanoid; A0T0X1; -.
DR   Proteomes; UP000001449; 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; 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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Chloroplast; Nucleotide-binding; Plastid;
KW   Reference proteome.
FT   CHAIN           1..602
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000275351"
SQ   SEQUENCE   602 AA;  65338 MW;  3339CE7297A26FB6 CRC64;
     MNKVVGIDLG TTNSVVAAIE GGQPTVITNA EGFRTTPSIV AYTKKQELLV GQLAKRQSVV
     NAENTFFSVK RFIGCKADEI SEESKELPYK VIKDSNGNIK IKCSSLNKDF SPEEISAQVI
     RKLIADAKEY LGQDVTKAVI TVPAYFNDSQ RQATVDAGKI AGIEVLRIIN EPTAASLAYG
     LDKKQNETIL VFDLGGGTFD VSILEVGDGI FEVLSTAGDT NLGGDDFDKA LVRWLVEDFE
     AKEGTNLTKD IQALQRLTEA AEKAKMELSN VEKTTINLPF ITADKNGPKH IQQELTREKF
     ESLCQDLINR CRIPVEKALK DAKLDQSGIN EVVLVGGSTR IPAIQQLVES LTGKKPNKSV
     NPDEVVAIGA AIQAGILAGE ITDILLLDVT PLSLGVETVG GIMTKLISRN TTIPVKKSEL
     FSTAADNQTN VEIHVLQGER EVVSGNKSLG NFKLEGIPQA PKGKPQIEVT FDINVDGILS
     VTAKENESGK EQNVTIQGAS NLSESEVNDM LEEAEKYAVI DKEQKEKSEM VVSATAYCDE
     VEKKLNSGEM GECTTEEEEE IKNVIKTLRE ALSSANYASI KESFEQLRTL TEVHLNSTNP
     AN