ID   DNAK_LISMC              Reviewed;         613 AA.
AC   C1KVC0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Lm4b_01483;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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; FM242711; CAS05245.1; -; Genomic_DNA.
DR   RefSeq; WP_003726023.1; NC_012488.1.
DR   AlphaFoldDB; C1KVC0; -.
DR   SMR; C1KVC0; -.
DR   KEGG; lmc:Lm4b_01483; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; LMON568819:LM4B_RS07395-MON; -.
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   Stress response.
FT   CHAIN           1..613
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205192"
FT   REGION          578..613
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   613 AA;  66158 MW;  66F429D2DA6CF662 CRC64;
     MSKIIGIDLG TTNSAVAVLE GGEAKIIPNP EGARTTPSVV GFKNGERQVG EVAKRAAITN
     PNTISSIKRH MGTNYKETIE GKDYSPQEIS AIILQYLKSY AEDYLGETVD KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAYGMDKTET DQTILVFDLG GGTFDVSILE
     LGDGVFEVHS TAGDNELGGD DFDKKIIDYL VAEFKKDNGI DLSQDKMALQ RLKDAAEKAK
     KDLSGVTSTQ ISLPFITAGE AGPLHLEVTL TRAKFDELTH DLVERTIAPT RQALKDANLS
     ASDIDQVILV GGSTRIPAVQ ETIKKELGKE PHKGVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IETMGGVMTT LIERNTTIPT SKSQTFSTAA DNQPAVDIHV LQGERPMAKD
     NKTLGRFQLA DIPPAPRGIP QIEVSFDIDK NGIVTVRAKD LGTGKEQNIV IKSSSGLTDE
     EIEKMVQDAE ANAEEDKKNK ENAELRNNAD QLVFTVDKTL KELEGKVEEE EVKKAEAARD
     ELQEALKGED FEAIKEKTES LNEIVQNLSV KLYEQAAAEQ QAAGGAEGQE APQNDDVVDA
     EFEEVNDDDK ENK