ID   DNAK_MAGMM              Reviewed;         653 AA.
AC   A0L4Z2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Mmc1_0510;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK43035.1; -; Genomic_DNA.
DR   RefSeq; WP_011712202.1; NC_008576.1.
DR   AlphaFoldDB; A0L4Z2; -.
DR   SMR; A0L4Z2; -.
DR   STRING; 156889.Mmc1_0510; -.
DR   PRIDE; A0L4Z2; -.
DR   EnsemblBacteria; ABK43035; ABK43035; Mmc1_0510.
DR   KEGG; mgm:Mmc1_0510; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002586; 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..653
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059596"
FT   REGION          608..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..653
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   653 AA;  69779 MW;  EE2DBFE6ABFE2D5E CRC64;
     MGKVVGIDLG TTNSCVSIME GGEPKVIENS EGVRTTPSMV AFTNQGERLV GQAAKRQAVT
     NPTNTLYAIK RLIGRRFSDP LTAKDQGLVP YKIVKADNGD AWVEADGKKM SPSECSAMIL
     QKMKQTAEDY LGESVSEAVI TVPAYFNDAQ RQATKDAGRI AGLEVLRIIN EPTAAALAYG
     LDKKDGQTIA VFDLGGGTFD ISILEIGDGV FEVKSTNGDT FLGGEDFDMA IIDYLADQFK
     KENSIDLRKD SMALQRLKEA AEKAKIELSS SNQTDINLPF ITADASGPKH LNLSLTRAKL
     ESLVDELVQR TLAPCRTALK DAGMTAADID EVILVGGMTR MPKVQAVVGQ FFGKEPHKGV
     NPDEVVAIGA AIQGGVLKGE VQDVLLLDVT PLSLGIETLG GVFTKLIEKN TTVPTRKSQV
     FSTAADNQSA VTIRVAQGER EMFSDNKTLG QFDLVGIAPA PRGMPQIEVT FDIDANGMVH
     VSAKDKGTGK EQSIHIEASG GLTSEEIDRM VHEAESHAEE DAKKRALIEA RNNADSLVYS
     SEKSLKEHSD KLDDALKNQI TAAIEDLKAV MPKEDPEAIS SKTQALMELS MKMGEQIYKE
     NPEAAGMDPE AAAHAAGMHG GAATGGGDGA NKHGKGAEDV VEAEFEEVND DKK