ID   DNAK_STAAB              Reviewed;         610 AA.
AC   Q2YT47;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SAB1452c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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; AJ938182; CAI81141.1; -; Genomic_DNA.
DR   RefSeq; WP_000034721.1; NC_007622.1.
DR   AlphaFoldDB; Q2YT47; -.
DR   SMR; Q2YT47; -.
DR   PRIDE; Q2YT47; -.
DR   KEGG; sab:SAB1452c; -.
DR   HOGENOM; CLU_005965_2_0_9; -.
DR   OMA; ISIKRHM; -.
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_1000059678"
FT   REGION          579..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..610
FT                   /note="Basic and 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   610 AA;  66321 MW;  0CA7322BB9F8BD31 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 SLIRRTMGPT RQAMKDAGLT
     NSDIDEVILV GGSTRIPAVQ EAVKKEIGKE TNKGVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IEILGGRMNT LIERNTTIPT SKSQIYSTAV DNQPSVDVHV LQGERPMAAD
     NKTLGRFQLT DIPPAERGKP QIEVTFDIDK NGIVNVTAKD LGTNKEQRIT IQSSSSLSDE
     EIDRMVKDAE VNAEADKKRR EEVDLRNEAD SLVFQVEKTL TDLGENIGEE DKKSAEEKKD
     ALKTALEGQD IEDIKSKKEE LEKVIQELSA KVYEQVAQQQ QQAQGANAGQ NNDSTVEDAE
     FKEVKDDDKK