ID   DNAK_LIGS1              Reviewed;         615 AA.
AC   Q1WUE8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=LSL_0578;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABD99387.1; -; Genomic_DNA.
DR   RefSeq; WP_011475828.1; NC_007929.1.
DR   RefSeq; YP_535470.1; NC_007929.1.
DR   AlphaFoldDB; Q1WUE8; -.
DR   SMR; Q1WUE8; -.
DR   STRING; 362948.LSL_0578; -.
DR   PRIDE; Q1WUE8; -.
DR   EnsemblBacteria; ABD99387; ABD99387; LSL_0578.
DR   KEGG; lsl:LSL_0578; -.
DR   PATRIC; fig|362948.14.peg.657; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000006559; 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; 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   Reference proteome; Stress response.
FT   CHAIN           1..615
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059591"
FT   REGION          575..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..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;  66614 MW;  764D2AAF94E1B806 CRC64;
     MSKIIGIDLG TTNSAVAVLE GKDPKIITNP EGNRTTPSVV SFKNGETQVG EVAKRQAITN
     PNTVSSIKRH MGDANYKVKI EDKEYTPQEI SAMILQYIKD YAESYLGEEV SQAVITVPAY
     FNDSQRQATK DAGKIAGLKV ERIVNEPTAA ALAYGLDKLD KDERILVFDL GGGTFDVSIL
     ELGDGVFEVL STNGDTHLGG DDFDNKIIDW LVENFKADNG IDLSQDKMAM QRLKDAAEKA
     KKDLSGTTEA QISLPFIAAG EAGPLHLETS LSRAKFNELT EDLVERTKIP VRNALADAGL
     TNADIDEVIL VGGSTRIPAV KEAVKAETGH TPNESVNPDE AVALGAAIQG GVITGDVKDV
     VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKSQVFSTA ADNQPAVDIH VLQGERPMAA
     DNKTLGRFQL TDIPVAPRGV PQIEVKFDID KNGIVNVSAK DLGTNKEQKI TIKSSSGLSD
     EEIDRMVKEA KENEAADKKR KEEVDLRNEV DQLLFQTDKT LKEVKDKVSA DEVKSVEDAR
     DALKKAQEQS DINEMKAKKD ELTKLIQDMS VKLYQQAQQA QQASGAQGDT SANNSTNDDN
     TVDGDFKEVD PDENK