ID   DNAK_LACCB              Reviewed;         624 AA.
AC   B3WEQ7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=LCABL_17780;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66858.1; -; Genomic_DNA.
DR   RefSeq; WP_003594633.1; NC_010999.1.
DR   AlphaFoldDB; B3WEQ7; -.
DR   SMR; B3WEQ7; -.
DR   KEGG; lcb:LCABL_17780; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..624
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119717"
FT   REGION          544..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..624
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   624 AA;  67564 MW;  33965C6F959AD3C4 CRC64;
     MSKVIGIDLG TTNSAVAVLE GNQPKIITNP EGNRTTPSVV AFKDGEIQVG EVAKRQAITN
     PDTIVSIKRH MGEANYKVKV GDKEYTPQEI SAMILQYIKK FSEDYLGEPV KDAVITVPAY
     FNDSQRQATK DAGKIAGLNV QRIINEPTAS ALAYGLDKGD KDEKILVYDL GGGTFDVSIL
     QLGDGVFEVL STNGDTHLGG DDFDNKIIDW LVAEFKKDNN IDLSKDKMAM QRLKDAAEKA
     KKDLSGVTQT QISLPFISAG PNGPLHLERT LTRAQFDEMT ADLVAKTKIP VENALKDAKL
     TNADIDKVIL NGGSTRTPAV QEAVKQWTGK DPDHSINPDE AVALGAAIQG GVISGDVKDV
     VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKSQVFSTA ADSQPAVDIH VLQGERPMAA
     DDKTLGRFEL TDIPPAPRGV PQIEVKFDID KNGIVQVSAK DLGTGKSQNI TIKSSSGLSD
     EEIERMKKEA EENADADEKR KEEVDLKNDV DQLLFQTDKT LKDVDGKVPE EDIKKVKDAQ
     EALKKAQQEN NLDDMKQKRD DLSKLVQDMT VKLYENAQKN QQAQGGPASG AATDAGAAQG
     SDDKKSDDDT INGDYKDVSD DDKK