ID   DNAK_MACCJ              Reviewed;         607 AA.
AC   B9E6X1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=MCCL_1232;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH17939.1; -; Genomic_DNA.
DR   RefSeq; WP_012657137.1; NC_011999.1.
DR   AlphaFoldDB; B9E6X1; -.
DR   SMR; B9E6X1; -.
DR   STRING; 458233.MCCL_1232; -.
DR   EnsemblBacteria; BAH17939; BAH17939; MCCL_1232.
DR   GeneID; 61128877; -.
DR   KEGG; mcl:MCCL_1232; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001383; 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; 2.
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..607
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000133151"
FT   REGION          577..607
FT                   /note="Disordered"
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   607 AA;  65402 MW;  F46C46C414ADA1BD CRC64;
     MSKVIGIDLG TTNSCVAVLE GGEPKVIANP EGNRTTPSVV AFKNGETQVG EVAKRQAITN
     PNTIISIKRH MGTDYKENIE GKEYSPQEIS AMILQNLKAT AESYLGEKVT KAVITVPAYF
     NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTDK EQKVLVFDLG GGTFDVSILE
     LGDGVFEVLS TSGDNKLGGD DFDQVIIDYL VEEFKKENGL DLSQDKMAMQ RLKDAAEKAK
     KDLSGVSSTQ ISLPFISAGE AGPLHLEVTL SRAKFEELSH TLVERTMGPT RQAMKDAGLS
     NADIDEVILV GGSTRIPAVQ EAIKKELGKE PNKGVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IETMGGVSTV LIERNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERQMAAD
     NKTLGRFQLT DIPPAPRGVP QIEVTFDIDK NGIVNVTAKD LGTQKEQKIT IQSSSSLSDE
     EIDRMVKDAE ANAEADKKRR EEVDLRNEAD QLVFATDKAI KDLEDKVDAA EKEKAEAAKE
     ELKKALEGND LEEIKAKKDT LNEIVQGLSM KLYEQMAQAQ QGAEGAASQD DDVVDADFTE
     VKDDDNK