ID   DNAK_PHATC              Reviewed;         613 AA.
AC   A0T0H7;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
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   Phaeodactylum tricornutum (strain CCAP 1055/1).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=556484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1;
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; EF067920; ABK20675.1; -; Genomic_DNA.
DR   RefSeq; YP_874452.1; NC_008588.1.
DR   AlphaFoldDB; A0T0H7; -.
DR   SMR; A0T0H7; -.
DR   STRING; 556484.A0T0H7; -.
DR   PRIDE; A0T0H7; -.
DR   GeneID; 4524555; -.
DR   InParanoid; A0T0H7; -.
DR   Proteomes; UP000000759; 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; 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; 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   Reference proteome.
FT   CHAIN           1..613
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000275349"
SQ   SEQUENCE   613 AA;  66724 MW;  CA2201B4B607DAA3 CRC64;
     MGKVVGIDLG TTNSVVAAIE GGQPSVIINA EGLRTTPSIV AYTKKEELLV GQIAKRQAVI
     NPENTFFSVK RFIGSKEGEI SKEAKKLPYK VSNDQNNNIK IKCPALNRDF SPEEISAQVL
     RKLINDATDY LGQEVTQAVI TVPAYFNDSQ RQATMDAGKI AGVEVLRIIN EPTAASLAYG
     LDKKQNETIL VFDLGGGTFD VSILEVGDGI FEVLSTAGDT NLGGDDFDNV LVNWLINDFK
     EKNNIDLGND VQALQRLTEA AEKAKVELST VEKTTIHLPF ITADKTGPKH IEQELTRDVF
     ENLCQALINR CRIPVEKSLN DARLDKADIN EIVLVGGSTR IPAVQNLVES LTGKKPNQSV
     NPDEVVAIGA AIQAGILAGE IKDILLLDVT PLSLGVETLG GVMTKIIARN TTIPVKKSEM
     FSTAVDNQTN VEIHILQGER ELVAGNKSLG NFRLDGIPAA DRGAPQIEVT FDIDVDGILS
     VKAREKETGV EQAVTIQGAS NLNEKEVEEM LVEAEKFASA DKVKRENIDV KNQAEALCFE
     AEKEVSSFND TVPENKKQNI KTLIENIRQA VQTDNFETLK EQMEELKTAM KDIVALKSTN
     DTATDPMSNL NDL