ID   DNAK_STAES              Reviewed;         609 AA.
AC   Q8CP17;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=SE_1267;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04866.1; -; Genomic_DNA.
DR   RefSeq; NP_764822.1; NC_004461.1.
DR   RefSeq; WP_002446567.1; NZ_WBME01000008.1.
DR   AlphaFoldDB; Q8CP17; -.
DR   SMR; Q8CP17; -.
DR   STRING; 176280.SE_1267; -.
DR   PRIDE; Q8CP17; -.
DR   EnsemblBacteria; AAO04866; AAO04866; SE_1267.
DR   KEGG; sep:SE_1267; -.
DR   PATRIC; fig|176280.10.peg.1236; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001411; 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   Stress response.
FT   CHAIN           1..609
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078543"
FT   REGION          525..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..609
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   609 AA;  66160 MW;  C4DC9E195C031666 CRC64;
     MGKVIGIDLG TTNSCVSILE GDEPKVIQNP EGARTTPSVV AFKNGETQVG EVAKRQAITN
     PNTVQSIKRH MGTDYKVDIE GKSYTPQELS AMILQNLKST AENYLGDTVD KAVITVPAYF
     NDGERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTET DQKVLVFDLG GGTFDVSILE
     LGDGVFEVLS TAGDNKLGGD DFDQVIIDYL VSEFKKENGV DLSQDKMALQ RLKDAAEKAK
     KDLSGVSQTQ ISLPFISAGE NGPLHLEISL TRSKFEELAD SLIKKTMEPT RQALKDAGLS
     TSEIDEVILV GGSTRIPAVQ EAVKKEIGKE PHKGVNPDEV VAMGAAIQAG VITGDVKDVV
     LLDVTPLSLG IEIMGGRMNT LIERNTTIPT SKSQVYSTAA DNQPAVDIHV LQGERPMASD
     NKTLGRFQLT DIPPAPRGVP QIEVTFDIDK NGIVNVTAKD LGTNKEQNIT IQSSSSLSDE
     EIDRMVKDAE ENAEADKKRR EEVDLRNEAD SLVFQVEKTV KDLGENISDE DKKNAEEKKD
     ALKTALEGED IDDIKAKKEE LEKVIQELSA KVYEQAQQAQ QQAQEEQGSQ DSTVEDADFK
     EVKDDEDKK