ID   DNAK_VIBHA              Reviewed;         640 AA.
AC   O87384;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9747709; DOI=10.1007/s004380050803;
RA   Klein G., Zmijewski M., Krzewska J., Czeczatka M., Lipinska B.;
RT   "Cloning and characterization of the dnaK heat shock operon of the marine
RT   bacterium Vibrio harveyi.";
RL   Mol. Gen. Genet. 259:179-189(1998).
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; AY639008; AAT39536.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87384; -.
DR   SMR; O87384; -.
DR   STRING; 669.AL538_12730; -.
DR   PRIDE; O87384; -.
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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078582"
FT   REGION          607..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   640 AA;  69077 MW;  470246409008B5FC CRC64;
     MGKIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTASVI AYTDGETLVG QPGGNVNAVT
     NPTRYTLFAI KRLIGRRFED EEVQRDIEIM PYKIVKADNG DAWVEAKGQK MAAPQVSAEV
     LKKMKKTAED FLGEEVTGAV ITVPAYFNDA QAQATKDAGR IAGLEVKRII NEPTAAALAY
     GLDKSGGDRT IAVYDLGGGT FDISIIEIDE VEGEKTFEVL ATNGDTHLGG EDFDNRLINY
     LVDEFNKEQG INLKNDPLAM QRVKEAAEKA KIELSSTSQT DVNLPYVTAD ATGPKHMNIK
     VTRAKLESLV EDLVQRSLEP LKVALADADL SVNDITDVIL VGGQTRMPMV QAKVAEFFGK
     EARRDVNPDE AVAMGAAVQG GVLAGEVKDV LLLDVTPLSL GIETMGAVMT KLVEKNTTIP
     TKANQVFSTA EDNQSAVTIH VLQGERKQAS FNKSLGQFNL EGIQAAPRGM PQIEVTFDLD
     ADGILHVSAK DKQTGKEQKI TIQASGGLSD DDIEKMVQEA EANKEADKKF EELATARNQA
     DQMIHGTRKQ VEEAGEALPA EEKEKIEAAI SELETARKGD DKEAIDAKVQ ALMTAAQKLM
     EIAQQQAQAQ QAQGGYAGAQ QSQEDDVVDA EFEEVKDDKK