ID   DNAK_NEOYE              Reviewed;         621 AA.
AC   Q1XDH2; Q1HDW3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
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   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Xu N.L., Yang R.;
RT   "Cloning hsp70 from Porphyra haitanesis and Porphyra yezoensis.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; DQ497595; ABF54971.1; -; Genomic_DNA.
DR   EMBL; AP006715; BAE92439.1; -; Genomic_DNA.
DR   RefSeq; YP_536996.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDH2; -.
DR   SMR; Q1XDH2; -.
DR   GeneID; 3978883; -.
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; 2.
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.
FT   CHAIN           1..621
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000275350"
FT   REGION          596..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        427
FT                   /note="P -> Q (in Ref. 1; ABF54971)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   621 AA;  67664 MW;  A59773A6F4141937 CRC64;
     MGKVVGIDLG TTNSVIAVME GGKPTVIPNA EGFRTTASVV AYTKSGDKLV GQIARRQAVI
     NPENTFYSVK RFIGRKQNEI SQEIRQTSYN VKTSGSSIKI ACPALNKDFA PEEISAQVLR
     KLVEDASTYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLDVLRIINE PTAASLSYGL
     DKQNNETILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDQQI VEWLIKDFKQ
     NEGIDLGKDR QALQRLTEAA EKAKIELSNL TQTEINLPFI TATQDGPKHL EKTVTRGKFE
     ELCSNLIDKC SIPVNNALKD AKLEASSIDE VVLVGGSTRI PAIQQMVKRL IGKDPNQSVN
     PDEVVAIGAA VQAGVLAGEV KDILLLDVTP LSLGVETLGG VMTKIIPRNT TIPTKKSEVF
     STAVDNPPNV EIQVLQGERE LTKDNKSLGT FRLDGIMPAP RGVPQIEVTF DIDANGILSV
     KAKEKATGKE QSITISGAST LPKDDVERMV KEAEENFDTD QKRRKNIDTK NQAESLCYQA
     EKQVKEFEDK ISQDLKIKIE ELITELRSSL EKEEYDNIES ISQQLQNALM DIGKNAAQTE
     SKDTKAKDDD TVIDTDFSEA K