ID   DNAK_LATSK              Reviewed;         613 AA.
AC   O87777;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Latilactobacillus sakei (Lactobacillus sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=1599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LTH681;
RX   PubMed=10553284; DOI=10.1016/s0723-2020(99)80039-3;
RA   Schmidt G., Hertel C., Hammes W.P.;
RT   "Molecular characterisation of the dnaK operon of Lactobacillus sakei
RT   LTH681.";
RL   Syst. Appl. Microbiol. 22:321-328(1999).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock as well as salt or ethanol stress.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AJ006274; CAA06941.1; -; Genomic_DNA.
DR   RefSeq; WP_016265325.1; NZ_SCIF01000014.1.
DR   AlphaFoldDB; O87777; -.
DR   SMR; O87777; -.
DR   GeneID; 57132140; -.
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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..613
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078476"
FT   REGION          577..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..613
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:0000250"
SQ   SEQUENCE   613 AA;  66276 MW;  1D9348482479A64F CRC64;
     MSKVIGIDLG TTNSAVAVLE GGQPKIITNP EGARTTPSVV SFKNGEIQVG EVAKRQAITN
     PDTIASIKRH IGEAGYKVTV GDKSYTPQEV SAMILQYIKK FAEDYLGEEV TEAVITVPAY
     FNDSQRQATK DAGKIAGLDV KRIINEPTAS ALAYGLDKTE TDEKVLVYDL GGGTFDVSVL
     ELGDGVFQVL STNGDTRLGG DDFDEAIMNW LVENFKSDNG IDLSKDKMAM QRLKDAAEKA
     KKDLSGVSST QISLPFISAG ENGPLHLEMT LSRTEFDRLT SDLVDRTKAP VMNALKDAGL
     DANEIDKVIL NGGSTRIPAV QEAVKNWTGK EPDHSINPDE AVALGAAVQG GVISGDVKDV
     VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKAQTFSTA ADNQPAVDIH VLQGERPMAA
     DNKTLGRFQL TDIPAAPRGV PQIEVKFDID KNGIVNVSAK DLGTNKEQKI TIKSNSGLSD
     EEIDRMMKEA QENEEADTKR KEEVDLKNDV DQLIFQTDKT LKELEGKVSD EELQKAKDAK
     EELVKAQQEN NLEDMKTKRD ALSEIVQELT VKLYQQAQEA QQAAGGAEGN ATDAKTDDGT
     VDGDFEEVKD DKE