ID   DNAK_LIMRD              Reviewed;         621 AA.
AC   A5VJE7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Lreu_0706;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82971.1; -; Genomic_DNA.
DR   RefSeq; WP_003668169.1; NZ_AZDD01000017.1.
DR   AlphaFoldDB; A5VJE7; -.
DR   SMR; A5VJE7; -.
DR   STRING; 557436.Lreu_0706; -.
DR   PRIDE; A5VJE7; -.
DR   EnsemblBacteria; ABQ82971; ABQ82971; Lreu_0706.
DR   GeneID; 66470847; -.
DR   KEGG; lre:Lreu_0706; -.
DR   PATRIC; fig|557436.17.peg.549; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001991; 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   Reference proteome; Stress response.
FT   CHAIN           1..621
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059590"
FT   REGION          476..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         176
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   621 AA;  67212 MW;  B8D1B38217BFE5EA CRC64;
     MASNKIIGID LGTTNSAVAV MEGNEPKIIT NPEGSRTTPS VVSFKNGETQ VGEVAKRQAI
     TNPNTISSIK SHMGEAGYTV EVDGKKYTPQ EISAMILQYL KKYAEDYIGD TVTQAVITVP
     AYFNDAQRQA TKDAGKIAGL DVKRIINEPT ASSLAYGLDK KDKDEKILVY DLGGGTFDVS
     ILELGDGVFQ VLSTNGDTHL GGDDFDQKIM DWLIDGFKEE HGVDLSQDKM ALQRLKDAAE
     KAKKDLSGVQ EAQISLPFIS AGENGPLHLE KTLSRAQFNQ LTNDLVERTK QPVLNALKDA
     DLTFDDIDEV ILNGGSTRIP AVQEMVKELT GKEPNHSINP DEAVALGAAI QGGVLTGDVK
     DVVLLDVTPL SLGIETMGGV FTKLIDRNTT IPTSKSQIFS TAADNQPAVD IHVLQGERPM
     AADNKTLGNF QLTDIPAAPR GVPQIKVTFD IDKNGIVNVS AEDQGTHKKQ NITIKSNSGL
     SDEEIERMKK DAEEHAEADK KKKEEVDLKN EVDQELFQVD KTLKEVKGKV PEDDIKKAES
     ARDELKKAKE SGNLDEMKAK KDALNKVIQD LSVKLYQQAQ GAQGGAANGQ PGDSQQNGND
     NGNDDNTVDG DFKDVTPDDK K