ID   DNAK2_PROMA             Reviewed;         633 AA.
AC   Q7V9G2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=Pro_1871;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00915.1; -; Genomic_DNA.
DR   RefSeq; NP_876262.1; NC_005042.1.
DR   RefSeq; WP_011126020.1; NC_005042.1.
DR   AlphaFoldDB; Q7V9G2; -.
DR   SMR; Q7V9G2; -.
DR   STRING; 167539.Pro_1871; -.
DR   PRIDE; Q7V9G2; -.
DR   EnsemblBacteria; AAQ00915; AAQ00915; Pro_1871.
DR   GeneID; 54201201; -.
DR   KEGG; pma:Pro_1871; -.
DR   PATRIC; fig|167539.5.peg.1973; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001420; 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   Reference proteome; Stress response.
FT   CHAIN           1..633
FT                   /note="Chaperone protein dnaK2"
FT                   /id="PRO_0000078513"
FT   REGION          600..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   633 AA;  68228 MW;  8B530FCECF855E2F CRC64;
     MGKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
     NPENTFYSAK RFVGRRVDEV NEESKEVSYS VEKSGSSVKL KCPVLDKQFS PEEVAAQVLR
     KLSEDAGKYL GENINQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DRKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDKVI VDHLAATFKA
     NEGIDLRQDK QALQRLTEAA EKAKIELSNA TQSEINLPFI TATPEGPKHV DLTLTRAKFE
     ELASNLIDRC RVPVEQALKD AKLSTGEIDE IVMVGGSTRM PAVKELVKRV TGKDPNQTVN
     PDEVVAVGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKMITRNT TVPTKKTETY
     STAVDGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPSP RGVPQIEVTF DIDANGILSV
     TAKDKGSGKE QSISITGAST LSDNEVEKMV KDAETNATAD KEKRDRIDIK NQAETLVYQT
     EKQLGELGDK VDEEAKAKVE AKRIQLKEAT EKDDYETMKT LVEDLQKELY SLGASVYQQS
     NAASQAADGT SSESNNSTEG NDDVIDAEFT ESK