ID   DNAK_VIBVU              Reviewed;         636 AA.
AC   Q8DF66;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=VV1_0357;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016795; AAO08882.1; -; Genomic_DNA.
DR   RefSeq; WP_011078453.1; NC_004459.3.
DR   AlphaFoldDB; Q8DF66; -.
DR   SMR; Q8DF66; -.
DR   PRIDE; Q8DF66; -.
DR   EnsemblBacteria; AAO08882; AAO08882; VV1_0357.
DR   KEGG; vvu:VV1_0357; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002275; Chromosome 1.
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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078585"
FT   REGION          600..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   636 AA;  68793 MW;  CB5D7A042158B24F CRC64;
     MGKIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTPSVI AYTDGETLVG QPAKRQAVTN
     PENTLFAIKR LIGRRFEDEE VQRDIEIMPY KIVKADNGDA WVEAKGQKMA APQVSAEVLK
     KMKKTAEDFL GEEVTGAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
     DKQGGDRTIA VYDLGGGTFD ISIIEIDEVE GEKTFEVLAT NGDTHLGGED FDNRLINYLV
     AEFKKDQGID LKNDPLAMQR VKEAAEKAKI ELSSTNQTDV NLPYITADAT GPKHMNIKVT
     RAKLESLVED LVQRSLEPLK VALADADLSV GDITDVILVG GQTRMPMVQA KVTEFFGKEP
     RRDVNPDEAV AVGAAVQGGV LAGDVKDVLL LDVTPLSLGI ETMGGVMTKL VEKNTTIPTK
     ANQVFSTAED NQSAVTIHVL QGERKQAMYN KSLGQFNLEG INPAPRGMPQ IEVTFDLDAD
     GILHVSAKDK QTGKEQKITI QASGGLSDAE IEKMVQEAEA NKEADKKFEE LATARNQADQ
     IIHGTRKQVE EAGEALPADE KAKIETAISE LEEARKGEDK EAIEAKIQAL MAAAQKLMEI
     AQQQAQAQQG SAEAGAQSQE DDVVDAEFEE VKDDKK