ID   DNAK_PELUB              Reviewed;         647 AA.
AC   Q4FNP9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=SAR11_0368;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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; CP000084; AAZ21190.1; -; Genomic_DNA.
DR   RefSeq; WP_006997539.1; NC_007205.1.
DR   AlphaFoldDB; Q4FNP9; -.
DR   SMR; Q4FNP9; -.
DR   STRING; 335992.SAR11_0368; -.
DR   PRIDE; Q4FNP9; -.
DR   EnsemblBacteria; AAZ21190; AAZ21190; SAR11_0368.
DR   GeneID; 66294866; -.
DR   KEGG; pub:SAR11_0368; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002528; 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..647
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225990"
FT   REGION          514..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   647 AA;  70040 MW;  CE0595593A8E6FCD CRC64;
     MSKIIGIDLG TTNSCVSIME GSQPKVLENA EGARTTPSVV AFTEDGEKLV GQPAKRQAVT
     NPENTIFAVK RLIGRSFEDP TVKKDIAAAP FKIVNSEKGD AWIEAKGEKY SPSQISAFIL
     QKMKETAEKY LGQEVTKAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAASLAYG
     LDKKQNKKIA VYDLGGGTFD VSILELGDGV FEVKSTNGDT FLGGEDFDNT IVDYLIGEFK
     KDSGIDLRSD KLALQRLKEA AEKAKIELSS AEQTDVNLPF ITADKTGPKH INLKMTRAKL
     EALVEDLISR TLPPCKTALK DAGLTASEID EIVMVGGMTR MPKVLSEVKN FFGKEPNKSV
     NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVSTKLIEKN TTIPTKKSQV
     FSTADDNQPA VSIRVLQGER EMASDNKMLG NFELVGIAPA PRGVPQIEVT FDIDANGIVS
     VSAKDKGTGK EQKIQIQASG GLSDEEIEKM VKDAEANKEE DKKKRESVDV RNQADTLLHS
     TEKNLKEHGA KVSDADKKAI EDASTDLKEA IKGTDTEEIK KKTETLVQAS MKLGEAIYKS
     QEKKEGSPKE GDKNDEGKKD DNVVDADFEE VKEESKEGKE EDKEKSA