ID   DNAK_OCEIH              Reviewed;         612 AA.
AC   Q8EPW4;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=OB1968;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13924.1; -; Genomic_DNA.
DR   RefSeq; WP_011066365.1; NC_004193.1.
DR   AlphaFoldDB; Q8EPW4; -.
DR   SMR; Q8EPW4; -.
DR   STRING; 221109.22777652; -.
DR   PRIDE; Q8EPW4; -.
DR   EnsemblBacteria; BAC13924; BAC13924; BAC13924.
DR   KEGG; oih:OB1968; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   PhylomeDB; Q8EPW4; -.
DR   Proteomes; UP000000822; 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; 2.
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..612
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078505"
FT   REGION          524..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..604
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   612 AA;  66558 MW;  5097482DC007BB41 CRC64;
     MSKIIGIDLG TTNSCVSVME GGEAVVIPNP EGNRTSPSVV AFKNGERQVG EVAKRQAITN
     PNTIQSIKRH MGTDYKVKIE EKEYTPQEVS AIILQYIKSY AEDYIGEKVE KAVITVPAYF
     NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGIDKEDQ DQTILVYDLG GGTFDVSILD
     IGDGTFEVVS TAGDNRLGGD DFDQVIIDHM VQEFKKENAI DLSQDKMATQ RLKDAAEKAK
     KDLSGVTQTQ ISLPFITAGD AGPLHLEMTM SRAKFDELSS DLVERTMQPT RKALSDASLS
     KSDIDKVILV GGSTRIPAVQ EAIKKELGQD PSKGVNPDEV VALGAAIQGG VLQGDVKDVL
     LLDVTPLSLG IETMGAVTTK LIERNTTIPT SASQTFSTAA DNQTAVDIHV LQGEREMASD
     NKTLGRFQLT DIPPAPRGMP QIEVSFDIDA NGIVNVRAKD LGTNKEQSIT IKSSSGLSDD
     EVDRMVKEAE ENADADKQRR EEVDLRNEAD QLIFTTDKTI KDLDDKVSEE DKQKAESAKD
     ELKQALESGD MEQVKAKKDA LEEHVQQLSA KLYEQVQQEA QQASGEQGEE SGNQDDDVVD
     ADYSEVDDDD KK