ID   DNAK_ALIFM              Reviewed;         634 AA.
AC   B5FA11;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=VFMJ11_2131;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) 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; CP001139; ACH66567.1; -; Genomic_DNA.
DR   RefSeq; WP_005420629.1; NC_011184.1.
DR   AlphaFoldDB; B5FA11; -.
DR   SMR; B5FA11; -.
DR   PRIDE; B5FA11; -.
DR   EnsemblBacteria; ACH66567; ACH66567; VFMJ11_2131.
DR   KEGG; vfm:VFMJ11_2131; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001857; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119774"
FT   REGION          601..634
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   634 AA;  68572 MW;  E0466B07C412376C CRC64;
     MGKIIGIDLG TTNSCVAVLD GDTPRVLENA EGERTTASVI AYTDGETLVG QPAKRQAVTN
     PQNTLFAIKR LIGRRFEDEE VQRDIEIMPF KIVKADNGDA WVEAKGQKMA APQVSAEVLK
     KMKKTAEDFL GEEVTGAVVT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAYGL
     DKKGGDRTIA VYDLGGGTFD ISIIEIDNVD GEQTFEVLAT NGDTHLGGED FDNRLINYLV
     SEFEKEQGIN LKNDPLAMQR VKEAAEKAKI ELSSAQQTDV NLPYVTADAT GPKHMNVKVT
     RAKLESLVED LVIRSLEPLK VALADSDLSV DEITDVILVG GQTRMPMVQA KVAEFFGKEA
     RRDVNPDEAV AMGAAVQGGV LAGDVKDVLL LDVTPLSFGI ETMGGVMTKL IEKNTTIPTK
     ADQTFSTAED NQSAVTIHVL QGERKQATYN KSLGQFNLEG IQPAPRGMPQ IEVTFDLDAD
     GILNVSAKDK STGKEQKITI QASGGLTDEE IEAMVQEAEA NKDADKKFEE LVTARNQADQ
     MIHGTQKQIE EAGDALPADE KEKIEAAIKA LEEVKSGNDK EAIDAKTQEL MQAAQKLMEI
     AQQKAQAQQG ADAGEQPKQD DDVVDAEFEE VKDK