ID   DNAK_LACJO              Reviewed;         624 AA.
AC   Q74IT6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=LJ_1479;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09247.1; -; Genomic_DNA.
DR   RefSeq; WP_004897147.1; NC_005362.1.
DR   AlphaFoldDB; Q74IT6; -.
DR   SMR; Q74IT6; -.
DR   STRING; 257314.LJ_1479; -.
DR   EnsemblBacteria; AAS09247; AAS09247; LJ_1479.
DR   KEGG; ljo:LJ_1479; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000581; 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; 1.
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..624
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225971"
FT   REGION          470..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..611
FT                   /note="Polar 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;  67117 MW;  F5B1081EE60338B8 CRC64;
     MSKVIGIDLG TTNSAVAVLE GKEPKIITNP EGNRTTPSVV AFKNGEIQVG EVAKRQAITN
     PNTIVSIKSH MGEEGYKVKV GDKEYTPQEI SAFILQYIKK FSEDYLGEKV TDAVITVPAY
     FNDAQRQATK DAGKIAGLNV QRIINEPTAS ALAYGLDKDE NDEKVLVYDL GGGTFDVSIL
     QLGDGVFQVL STNGDTHLGG DDFDQRIMDW LIQNFKEENG VDLSNDKMAL QRLKDAAEKA
     KKDLSGVSST HISLPFISAG EAGPLHLEAD LTRAKFDELT DDLVQKTKVA FDNALSDAGL
     TVNDIDKVIL NGGSTRIPAV QKAVKDWAGK EPDHSINPDE AVALGAAIQG GVISGDVKDI
     VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKSQIFSTA ADNQPAVDVH VLQGERPMAA
     DDKTLGRFEL TDIPPAPRGV PQIQVTFDID KNGIVNVSAK DMGTGKEQKI TIKSSSGLSD
     EEIKKMQKDA EEHAEEDKKR KEEVDLRNEV DQLIFTTEKT LKETEGKVPE TETKNVQDAL
     DALKKAQKDN NLDEMKEKKE ALSKAAQDLA VKLYQQNGGA QGAAGQAGPQ GPQNGGQPNN
     DNGSDNGQGG STVDGDFHKV DPDK