ID   DNAK_VIBPA              Reviewed;         637 AA.
AC   Q87RX3;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=VP0653;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58916.1; -; Genomic_DNA.
DR   RefSeq; NP_797032.1; NC_004603.1.
DR   RefSeq; WP_005455943.1; NC_004603.1.
DR   AlphaFoldDB; Q87RX3; -.
DR   SMR; Q87RX3; -.
DR   STRING; 223926.28805639; -.
DR   PRIDE; Q87RX3; -.
DR   EnsemblBacteria; BAC58916; BAC58916; BAC58916.
DR   GeneID; 1188128; -.
DR   KEGG; vpa:VP0653; -.
DR   PATRIC; fig|223926.6.peg.623; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002493; 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   Reference proteome; Stress response.
FT   CHAIN           1..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078583"
FT   REGION          600..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..615
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   637 AA;  69055 MW;  EBC916213B1F7F00 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 LKNDPLAMQR VKEAAEKAKI ELSSTSQTDV NLPYVTADAT GPKHMNIKVT
     RAKLESLVED LVQRSLEPLK VALADADLSV NDITDVILVG GQTRMPMVQA KVAEFFGKEA
     RRDVNPDEAV AMGAAVQGGV LAGEVKDVLL LDVTPLSLGI ETMGGVMTKL VEKNTTIPTK
     ANQVFSTAED NQSAVTIHVL QGERKQAMYN KSLGQFNLEG IQPAPRGMPQ IEVTFDLDAD
     GILHVSAKDK QTGKEQKITI QASGGLSDDE IEKMVQEAEA NKEADKKFEE LATARNQADQ
     MIHGTRKQME EAGDALPAEE KEKIETAISE LEEARKGEDK EAIDAKVQAL MTAAQKLMEI
     AQQQAQAQQA QGADAGAQSK DDDVVDAEFE EVKDDKK