ID   DNAK_HAHCH              Reviewed;         642 AA.
AC   Q2SMM8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=HCH_01224;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC28096.1; -; Genomic_DNA.
DR   RefSeq; WP_011395169.1; NC_007645.1.
DR   AlphaFoldDB; Q2SMM8; -.
DR   SMR; Q2SMM8; -.
DR   STRING; 349521.HCH_01224; -.
DR   PRIDE; Q2SMM8; -.
DR   EnsemblBacteria; ABC28096; ABC28096; HCH_01224.
DR   KEGG; hch:HCH_01224; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000238; Chromosome.
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..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059574"
FT   REGION          578..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..642
FT                   /note="Basic and acidic 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   642 AA;  68898 MW;  6C51D047CC6C37DC CRC64;
     MGKIIGIDLG TTNSCVAILE GDKPRVIENS EGGRTTPSIV AYTDDETLVG QSAKRQAVTN
     PTNTLFAIKR LIGRRFEDDV VQKDIKMVPY TIAKADNGDA WVDVKGKKMA PPQISAEVLK
     KMKKTAEDFL GEKVTEAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAALAYGM
     DKKGGDRKVA VYDLGGGTFD ISIIEIADVD GEMQFEVLAT NGDTFLGGED FDLRLIDYLA
     QEFKKDSGID LKGDPLAMQR LKEAAEKAKI ELSSSQQTDV NLPYITADAS GPKHLNVKVT
     RAKLESLVEE LVERSLEPCR IALKDSGCSS SEIDEVILVG GQTRMPLVQS KVADFFGKEA
     RKDVNPDEAV AIGAAIQGAV LSGDVKDVLL LDVTPLSLSI ETMGGVSTPI IEKNTTIPTK
     KSQVFSTAED NQTAVTIHVL QGERKQAQMN KSLGRFDLTG LPPAPRGVPQ VEVTFDIDAN
     GIMHVSAKDK ATGKEQSIVI KASSGLSEDE IDKMVQDAEA HAAEDKKFEE LAASRNQADA
     LVHATQKTLK DAGDKVTAEE KVAIEAAIKE LEEAIKGDDK EAIESRMQKL SEASSSMAQK
     MYAEQAAQQG GDAGAQAEDA AGKPADDAVD AEFEEVKDGD KK