ID   DNAK_TETHA              Reviewed;         618 AA.
AC   Q93R27;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, 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};
OS   Tetragenococcus halophilus (Pediococcus halophilus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Tetragenococcus.
OX   NCBI_TaxID=51669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fukuda D., Watanabe M., Sonezaki S., Sugimoto S., Sonomoto K., Ishizaki A.;
RT   "Characterization and expression analysis of dnaK operon of halophilic
RT   lactic acid bacterium Tetragenococcus halophila.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
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; AB070346; BAB63290.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93R27; -.
DR   SMR; Q93R27; -.
DR   BRENDA; 3.6.4.10; 4579.
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   Stress response.
FT   CHAIN           1..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078571"
FT   REGION          573..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..618
FT                   /note="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   618 AA;  66784 MW;  929D8937F122478E CRC64;
     MSKIIGIDLG TTNSAVSVLE GGESQIITNP EGNRTTPSAV AFKNGEIQVG EVAKRQAVTN
     SDTVTSIKRH IGEDGYKVEA NNKSYTPQEI SAMILQHIKS FSEDYLGEEV EKAVITVPAY
     FNDSQRQATK DAGKIAGLEV ERIVNEPTAA ALAYGLDKTE QDEKILVFDL GGGTFDVSIL
     ELGDGVFDVL STAGDNKLGG DDFDEKIIDY MVSEFKKENG IDLSKDKMAL QRLKDAAEKA
     KKDLSGVSST QISLPFITAG EDGPLHLEMN MTRAKFDELT SSLVDRTKEP VRQALKDADL
     SQSDIDQVIL VGGSTRIPSV VESVRKETGK EPNKSVNPDE VVAMGAAIQA GVISGDVKDV
     VLLDVTPLSL GIETMGGVFT KLIDRNTTIP TSKSQVFSTA ADNQPAVDIH VLQGERPMAA
     DNKTLGRFQL TDIPAAPRGV PQIEVSFDID KNGIVNVSAK DLGTQKRTKI TIQSSSGLSD
     DEIDKMVKDA EANAEADEKR KEEVDLRNEV DTLLFTVDKT LSDLDGKVDE EEVKKAENAR
     DELKAAVEAD DIEDMKTKRD ALNEIVQNLS VKMYEQASQE QQGDQAAQGS DDASNASGDD
     DVVDADFEEV DDDDNDNQ