ID   DNAK_STAAU              Reviewed;         610 AA.
AC   P45554;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=912;
RX   PubMed=8045913; DOI=10.1128/jb.176.15.4779-4783.1994;
RA   Ohta T., Saito K., Kuroda M., Honda K., Hirata H., Hayashi H.;
RT   "Molecular cloning of two new heat shock genes related to the hsp70 genes
RT   in Staphylococcus aureus.";
RL   J. Bacteriol. 176:4779-4783(1994).
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; D30690; BAA06359.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45554; -.
DR   SMR; P45554; -.
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   Stress response.
FT   CHAIN           1..610
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078542"
FT   REGION          578..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   610 AA;  66347 MW;  B34745C36D26AAED CRC64;
     MSKIIGIDLG TTNSCVTVLE GDEPKVIQNP EGSRTTPSVV AFKNGETQVG EVAKRQAITN
     PNTVQSIKRH MGTDYKVDIE GKSYTPQEIS AMILQNLKNT AESYLGEKVD KAVITVPAYF
     NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTDK DEKVLVFDLG GGTFDVSILE
     LGDGVFEVLS TAGDNKLGGD DFDQVIIDYL VAEFKKENGV DLSQDKMALQ RLKDAAEKAK
     KDLSGVSQTQ ISLPFISAGE NGPLHLEVNL TRSKFEELSD SLIRRTMEPT RQAMKDAGLT
     NSDIDEVILV GGSTRIPAVQ EAVKKEIGKE PNKGVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IEILGGRMNT LIERNTTIPT SKSQIYSTAV DNQPSVDVHV LQGERPMAAD
     NKTLGRFQLT DIPPAERGKP QIEVTFDIDK NGIVNVTAKD LGTNKEQRIT IQSSSSLSDE
     EIDRMVKDAE VNAEADKKRR EEVDLRNEAD SLVFQVEKTL TDLGENIGEE DKKSAEEKKD
     ALKTALEGQD IEDIKSKKEE LEKVIQELSA KVYEQAAQQQ QQAQGANAGQ NNDSTVEDAE
     FNEVKDDDKK