ID   DNAK_VIBC1              Reviewed;         638 AA.
AC   A7MWW0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
GN   OrderedLocusNames=VIBHAR_01134;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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; CP000789; ABU70124.1; -; Genomic_DNA.
DR   RefSeq; WP_012127136.1; NC_022269.1.
DR   AlphaFoldDB; A7MWW0; -.
DR   SMR; A7MWW0; -.
DR   PRIDE; A7MWW0; -.
DR   EnsemblBacteria; ABU70124; ABU70124; VIBHAR_01134.
DR   KEGG; vha:VIBHAR_01134; -.
DR   PATRIC; fig|338187.25.peg.1494; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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_1000059697"
FT   REGION          603..638
FT                   /note="Disordered"
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   638 AA;  68952 MW;  078EBDB263B924E3 CRC64;
     MGKIIGIDLG TTNSCVAVLD GDKPRVIENA EGERTTASVV AYTDGETLVG QPAKRQAVTN
     PTNTLFAIKR LIGRRFEDEE VQRDIEIMPY KIVKADNGDA WVEAQGQKMA APQVSAEILK
     KMKKTAEDFL GEEVTGAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGL
     DKSGGDRTIA VYDLGGGTFD ISIIEIDEVE GEKTFEVLAT NGDTHLGGED FDTRLINYLV
     DEFNKEQGIN LKNDPLAMQR VKEAAEKAKI ELSSTSQTDV NLPYVTADAT GPKHMNVKVT
     RAKLESLVED LVQRSLEPLK VALADADLSV NDITDVILVG GQTRMPMVQA KVAEFFGKEA
     RRDVNPDEAV AMGAAVQGGV LAGDVKDVLL LDVTPLSLGI ETMGGVMTKL VEKNTTIPTK
     ANQVFSTAED NQSAVTIHVL QGERKQASFN KSLGQFNLEG IQAAPRGMPQ IEVTFDLDAD
     GILHVSAKDK QTGKEQKITI QASGGLSDED IEKMVQEAEA NKEADKKFEE LAAARNQADQ
     MIHGTRKQVE EAGEALPAEE KEKIEAAISE LETARKGDDK EAIDAKVQAL MTAAQKLMEI
     AQQQAQAQQA QGADADAQQS KEDDVVDAEF EEVKDDKK