ID   DNAK_VIBPR              Reviewed;         637 AA.
AC   Q9L7Z1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 79.
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 proteolyticus (Aeromonas proteolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Galkin A., Yoshimune K., Kulakova L., Yoshimura T., Esaki N.;
RT   "DnaK from marine bacterium Vibrio proteolyticus: novel dnaK locus
RT   organization and the protein characterization.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AF218211; AAF27648.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L7Z1; -.
DR   SMR; Q9L7Z1; -.
DR   PRIDE; Q9L7Z1; -.
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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078584"
FT   REGION          606..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   637 AA;  68987 MW;  F93D9DDC534DA60B CRC64;
     MGKIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTASVI AYTDGETLVG QPAKRQAVTN
     PTNTLFAIKR LIGRRFEDEE VQRDIEIMPY KIVKADNGDA WVEAKGQKMA APQVSAEVLK
     KMKKTAEDFL GEEVTGAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
     DKKGGDRTIA VYDLGGGTFD ISIIEIDEVE GEKTFEVLAT NGDTHLGGED FDNRLINYLV
     DEFKKEQGID LKTDPLAMQR VKEAAEKAKI ELSFTSQTDV NLPYVTADAT APKHMNVKVT
     RAKLESLVED LVQRSLEPLK VALADADLSV NDITDVILVG GQTRMPMVQA KVAEFFGKEA
     RRDVNPDEAV AMGAAVQGGV LAGDVKDVLL LDVTPLSLGI ETMGGVMTKL VEKNTTIPTK
     ANQVFSTAED NQSAVTIHVL QGERKQAMYN KSLGQFNLEG IQPAPRGMPQ IEVTFDLDAD
     GILHVSAKDK QTGKEQKITI QASGGLSDDE IEKMVQEAEA NKEADKKFEE LATARNQADQ
     MIHGTRKQVE EAGDALPAED KEKIEAAVSE LEDARKGDDK EAIDAKVQAL MTASQKLMEI
     AQQQAQAQAA QGGDEAAQSK DDDVVDAEFE EVKDDKK