ID   DNAK_PROMT              Reviewed;         630 AA.
AC   Q46I76;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
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}; OrderedLocusNames=PMN2A_1313;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; CP000095; AAZ58802.1; -; Genomic_DNA.
DR   RefSeq; WP_011295656.1; NC_007335.2.
DR   AlphaFoldDB; Q46I76; -.
DR   SMR; Q46I76; -.
DR   STRING; 59920.PMN2A_1313; -.
DR   PRIDE; Q46I76; -.
DR   EnsemblBacteria; AAZ58802; AAZ58802; PMN2A_1313.
DR   KEGG; pmn:PMN2A_1313; -.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 161217at2; -.
DR   PhylomeDB; Q46I76; -.
DR   Proteomes; UP000002535; 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; 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..630
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225994"
FT   REGION          601..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   630 AA;  67881 MW;  EDFBA42EAAFED052 CRC64;
     MGKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV AYTKNQDQLV GQIAKRQAVM
     NPENTFYSSK RFVGRRVDEV NDESKEVSYG VEKAGSNVKI KCPILDKQFS PEEVSAQVLR
     KLSDDAGKYL GETVTQAVIT VPAYFNDSQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKSNERILV FDLGGGTFDV SVLEVGDGVF EVLSTSGDTH LGGDDFDRVI VDHLASTFKG
     NEGIDLRQDK QALQRLTEAA EKAKIELSNA TQSEINLPFI TATPEGPKHL DLTLTRGKFE
     ELASNLIDRC RVPVEQALKD AKLSTGEIDE IVMVGGSTRM PAVKELVKRV TTKDPNQTVN
     PDEVVAVGAA IQGGVLAGEV KDILLLDVTP LSLGVETLGG VMTKMISRNT TVPTKKAETY
     STAVDGQTNV EIHVLQGERE MASDNKSLGT FRLDGIPPAP RGVPQIEVTF DIDANGILSV
     NAKDKGSGKE QSISITGAST LSDNEVDKMV KDAEMNASAD KEKREKIDIK NQAETLVYQA
     EKQIGELGDK VDEAAKAKVE EKRIKLKEAT EKDDYESMKT LVEELQQELY SLGASVYQQA
     NDASQAAADS NTDSKVDGDD VIDADFTETK