ID   DNAK_LEUCK              Reviewed;         596 AA.
AC   B1MZG6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=LCK_01091;
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20;
RX   PubMed=18281406; DOI=10.1128/jb.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82918.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1MZG6; -.
DR   SMR; B1MZG6; -.
DR   STRING; 349519.LCK_01091; -.
DR   PRIDE; B1MZG6; -.
DR   EnsemblBacteria; ACA82918; ACA82918; LCK_01091.
DR   KEGG; lci:LCK_01091; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002166; 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; 1.
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..596
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119725"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   596 AA;  63384 MW;  79BC2BA207B7B086 CRC64;
     MSKIIGIDLG TTNSAVAVLE GGEPKIITNP DGGRTTPSVV SFKNGESQVG DVAKRQAITN
     PDTIISIKSH MGEAGYKVTA DGKDYTPQEI SAMILQYIKG YAEDYLGEKV EKAVITVPAY
     FNDAQRQATK DAGKIAGLEV ERIINEPTAA ALAYGLDKLD KDEKILVYDL GGGTFDVSIL
     ELGDGVFEVL STNGDTHLGG DDFDNKIIDY LAAQFKADNG IDLKDDKLAL QRLKDAAESA
     KKTLSSANEA QIDLPFIASG DQGPLHLQTS LSRAKFNELT ADLIKKAEQP VLNALKDAGL
     SFSDIDEVIL NGGSTRIPAV QESVKKLTGK EPNHSINPDE AVALGAAVQG GVITGDVKDV
     VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKSQVFSTA ADNQPAVDIH VLQGERSMAA
     DNKTLGRFQL SDIPAAKRGV PQIEVTFDID RNGIVSVSAK DLGTQKEQKI TIQAAGGLSE
     EEIEQMMNDA KANEEADAKK KEAVDTRNEA DQLIFSTEAT LEEAGDKLSD DDKKATQEAL
     EALKKAKEDA AAEDADLTDL KAKTEALAKA AQELAMKLYQ QAAPKEGAEG EAKPKG