ID   DNAK_NEOHI              Reviewed;         621 AA.
AC   Q06W39;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
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   Neoporphyra haitanensis (Red seaweed) (Porphyra haitanensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neoporphyra.
OX   NCBI_TaxID=1262161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Xu L., Yang R., Sun X.;
RT   "Cloning hsp70 from Porphyra haitanesis and Porphyra yezoensis.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ480726; ABF20063.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q06W39; -.
DR   SMR; Q06W39; -.
DR   PRIDE; Q06W39; -.
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.
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_0000277263"
FT   REGION          598..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  67725 MW;  DA81DC9226533F79 CRC64;
     MGKVVGIDLG TTNSVIAVME GGKPTVIPNA EGFRTTASVV AYTKSGDKLV GQIARRQAVI
     NPENTFYSVK RFIGRKQNEI SQEIRQTSYN VKTSGSSIKI ACPALDKDFA PEEISAQVLR
     KLVEDASTYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLDVLRIINE PTAAPLSYGL
     DKQNNETILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDQQI VEWLIKDFKQ
     NEGIDLAKDR QALQRLTEAA EKAKIELSNL TQTEINLPFI TATQDGPKHL EKTVTRGKFE
     ELCSNLIDKC SIPVNNALKD AKLEASSIDE VVLVGGSTRI PAIQQMVKRL IGKDPNQSVN
     PDEVVAIGAA VQAGVLAGEV KDILLLDVTP LSLGVETLGG VMTKIIPRNT TIPTKKSEVF
     STAVDNQPNV EIQVLQGERE LTKDNKSLGT FRLDGIMPAP RGVPQIEVTF DIDANGILSV
     KAKEKATGKE QSITISGAST LPKDDVERMV KEAEENFDTD QKRRKNIDTK NQAESLCYQA
     EKQIKEFEDK ISQDLKTKIE ELITELRSSL EKEEYENIES ISQRLQNSLM DIGKMAAQAE
     SKNTNTKDDG TVIDTDFSEA K