ID   DNAK_LIMF3              Reviewed;         618 AA.
AC   B2GBQ5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=LAF_0751;
OS   Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS   fermentum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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; AP008937; BAG27087.1; -; Genomic_DNA.
DR   RefSeq; WP_003685154.1; NC_010610.1.
DR   AlphaFoldDB; B2GBQ5; -.
DR   SMR; B2GBQ5; -.
DR   EnsemblBacteria; BAG27087; BAG27087; LAF_0751.
DR   GeneID; 61201164; -.
DR   KEGG; lfe:LAF_0751; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001697; 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..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119718"
FT   REGION          526..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..618
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   618 AA;  67124 MW;  362C4AFACEFEAD57 CRC64;
     MASNKIIGID LGTTNSAVAV MEGNEPKIIT NPEGGRTTPS VVSFKNGEVQ VGEVAKRQAI
     TNPNTVKSIK SHMGEAGYTV DIEGKKYTPQ EISAMILQYI KKYAEDYIGD TVTEAVITVP
     AYFNDAQRQA TKDAGKIAGL DVKRIINEPT ASSLAYGLDK KDRDEKILVY DLGGGTFDVS
     ILELGDGVFQ VLSTNGDTHL GGDDFDQKIM DWLIDGFKQE NGIDLSQDKM ALQRLKDAAE
     KAKKDVSGVQ EAQISLPFIT SGDNGPLHLE KTLTRAQFNQ LTNDLVERTK QPVLNALKDA
     ELSFSDIDEV ILNGGSTRIP AVQEMVKSLT GKEPNHSINP DEAVALGAAI QGGVLTGDVK
     DVVLLDVTPL SLGIETMGGV FTKLIDRNTT IPTSKSQVFS TAADNQPAVD IHVLQGERPM
     AADNKTLGNF QLTDIPPAPR GVPQIKVTFD IDKNGIVNVS AEDQGTHKKQ NITIKSNSGL
     SDEEIERMKK DAEANAEADK KKKEEADLRN ETDQLLFQTD KTLEELKGKV SDDEIKKAQD
     AKDALQKAKD DNNLEDMKAK KDDLNKIVQD LTVKLYQQAQ QENQANGGQP TGDQGDGKKD
     DDNTVDGDFE EVNPDDKK