ID   DNAK2_PARMW             Reviewed;         637 AA.
AC   Q7U3C4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein dnaK2;
DE   AltName: Full=HSP70-2;
DE   AltName: Full=Heat shock 70 kDa protein 2;
DE   AltName: Full=Heat shock protein 70-2;
GN   Name=dnaK2; OrderedLocusNames=SYNW2508;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BX569695; CAE09023.1; -; Genomic_DNA.
DR   RefSeq; WP_011129361.1; NC_005070.1.
DR   AlphaFoldDB; Q7U3C4; -.
DR   SMR; Q7U3C4; -.
DR   STRING; 84588.SYNW2508; -.
DR   PRIDE; Q7U3C4; -.
DR   EnsemblBacteria; CAE09023; CAE09023; SYNW2508.
DR   KEGG; syw:SYNW2508; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001422; Chromosome.
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; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein dnaK2"
FT                   /id="PRO_0000078567"
FT   REGION          602..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   637 AA;  67888 MW;  CE29E880E7D1B5D9 CRC64;
     MGKVVGIDLG TTNSCVSVME GGKPTVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
     NPDNTFYSVK RFIGRRVDEV NEESKEVSYG VEKAGSNVKV KCPVLDKQFA PEEVSAQVLR
     KLAEDAGKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDKVI VDHLAETFKS
     NEGIDLRQDK QALQRLTEAA EKAKIELSSA TQSEINLPFI TATPEGPKHL DLTLTRAKFE
     ELAANLIDRC RIPVEQALKD AKLSSSELDE IVMVGGSTRI PAVLELVKRT TSKDPNQTVN
     PDEVVAVGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKMITRNT TVPTKKTETY
     STAVDGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPAP RGVPQIEVTF DIDANGILSV
     TAKDKGSGKE QSISITGAST LSDSEVDKMV KDAEANASAD KEKREKIDLK NQAETLVYQA
     EKQMGELGDK VEADAKAKVD EKRTKLQEAI NAEDYDAMKT LLEELQQELY TVGASVYQQE
     GAAAGGAAPG GDAGASAASG GGDASDDVID AEFTETK