ID   DNAK_PRELO              Reviewed;         638 AA.
AC   Q93GF1;
DT   15-MAY-2002, 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;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Prevotella loescheii.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=840;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11136127; DOI=10.1007/s0028403313;
RA   Manch-Citron J.N., Shahani P.J., Schneider R.;
RT   "Cloning, characterization, and possible origin of the Prevotella loescheii
RT   dnaK homolog.";
RL   Curr. Microbiol. 42:82-88(2001).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF252852; AAL08408.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93GF1; -.
DR   SMR; Q93GF1; -.
DR   PRIDE; Q93GF1; -.
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; 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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078510"
FT   REGION          597..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   638 AA;  68072 MW;  BB53C43C502EC477 CRC64;
     MGKIIGIDLG TTNSCVAVFE GNEPVVIANS EGKRTTPSVV GFVKDGERKV GDPAKRQAIT
     NPKNTVYSIK RFMGETYEQS RKEAEAMPYT VINENGLPRV DIEGRKYTPQ EISAMILQKM
     KKTAEDYLGQ EVTDAVITVP AYFSDSQRQA TKEAGQIAGL NVQRIVNEPT AAALAYGVDK
     GNKDMKIAVF DLGGGTFDIS ILEFGGGVFE VLSTNGDTHL GGDDFDQVII KWLADGFKAD
     EGIDLTKDPM AMQRLKEAAE KAKIELSSTT STEINLPYIS AEGGVPKHLV KTLTRAQFEQ
     LAHDLIQACL VPCQNAIKDA KLSTSDIDEV ILVGGSSRIP AVQTLVKNYF GKEPSKGVNP
     DEVVAVGAAI QGAILNKESG VGDIVLLDVT PLTLGIETMG GVMTKLIDAN TTIPHKKSET
     FSTAVDNQTA VTIHVLQGER PMASQNKSIG QFNLEGIAPA RRGVPQIEVT FDIDANGILN
     VSAKDKATGK EQKIRIEASS GLSKEEIERM KAEAEQNAAA DKAEREKVDK LNQADSMIFT
     TENFLKDNGD KIPADQKPGI ESALQQLKDA HKAADVAAID AAINNLNSVM QAASAQMYQG
     AGGAQPDPNA GFQGAGGEQA QGGSTGDNVQ DADFEEVK