ID   DNAK_LEUMM              Reviewed;         615 AA.
AC   Q03WI2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=LEUM_1347;
OS   Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS   20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS   8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=203120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC   / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000414; ABJ62440.1; -; Genomic_DNA.
DR   RefSeq; WP_011680047.1; NC_008531.1.
DR   AlphaFoldDB; Q03WI2; -.
DR   SMR; Q03WI2; -.
DR   STRING; 203120.LEUM_1347; -.
DR   PRIDE; Q03WI2; -.
DR   EnsemblBacteria; ABJ62440; ABJ62440; LEUM_1347.
DR   GeneID; 61176174; -.
DR   KEGG; lme:LEUM_1347; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000362; 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   Stress response.
FT   CHAIN           1..615
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000072037"
FT   REGION          581..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   615 AA;  65691 MW;  5338E8FA0D4AE5BA CRC64;
     MSKIIGIDLG TTNSAVAVLE GGEPKIITNP DGGRTTPSVV SFKNGESQVG DVAKRQAITN
     PDTIISIKSH MGEAGYKVNA NGKDYTPQEI SAMILQYIKG YAEDYLGEKV EKAVITVPAY
     FNDAQRQATK DAGKIAGLEV ERIINEPTAA ALAYGLDKLD KDEKILVYDL GGGTFDVSIL
     ELGDGVFEVL STNGDTHLGG DDFDNKVIDY LAEQFKSENG VDLKDDKLAL QRLKDAAESA
     KKTLSSANEA QIDLPFIASG DNGPLHLQTS LTRAKFNELT ADLIKKAEQP VLSALKDAGL
     SFSDIDEVIL NGGSTRIPAV QESVKKMTGK EPNHSINPDE AVALGAAVQG GVITGDVKDV
     VLLDVTPLSL GIETMGGVFT KLIERNTTIP TSKSQVFSTA ADNQPAVDIH VLQGERSMAA
     DNKTLGRFQL ADIPAAPRGV PQIEVTFDID RNGIVNVSAK DLGTQKEQKI TIQAAGGLSD
     EEIEKMMNDA KANEEADAKK KEAVDTRNEA DQLIFQTEKT LEEVGDKLGD DEKKPTQDAL
     EALKKAKEDA AADDADLTDL KAKSEELTKV AGELAMKLYQ QAAPKDGAEG DAKSADDNTV
     DGDFEEVDPN KDDKK