ID   DNAK_MARN8              Reviewed;         641 AA.
AC   A1U614;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Maqu_3362;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM20433.1; -; Genomic_DNA.
DR   RefSeq; WP_011786774.1; NC_008740.1.
DR   AlphaFoldDB; A1U614; -.
DR   SMR; A1U614; -.
DR   STRING; 351348.Maqu_3362; -.
DR   PRIDE; A1U614; -.
DR   EnsemblBacteria; ABM20433; ABM20433; Maqu_3362.
DR   KEGG; maq:Maqu_3362; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000998; 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   Stress response.
FT   CHAIN           1..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059597"
FT   REGION          602..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69369 MW;  518D91936F3A8073 CRC64;
     MSKIIGIDLG TTNSCVAIMD GDKVKVIENA EGDRTTPSII AYTDDNETLV GQSAKRQAVT
     NPHNTLYAIK RLIGRRFEDD VVQKDIKMVP YKIAKADNGD AWVEVKGQKM APPQVSAEVL
     KKMKKTAEDY LGEKVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
     LDKKSGDRTV AVYDLGGGTF DLSIIEIADV DGEHQFEVLA TNGDTFLGGE DFDLKVIEYL
     ADQFKKDSGI DLRGDSLAMQ RLKEAAEKAK IELSSSQQTD VNLPYITADA SGPKHMNVKL
     TRAKLESLVE DLVQRSLEPC KVALQDAGMK AGEIDEVILV GGQTRMPLVQ EKVKEFFGKE
     PRKDVNPDEA VAMGAAIQGA VLSGDVKDVL LLDVTPLTLG IETMGGVATP LIEKNTTIPT
     KKSQIFSTAD DNQTAVTIHV VQGERKQAAQ NKSLGRFDLA DIPPAPRGVP QIEVTFDIDA
     NGILNVSAKD KATGKEQSIV IKASSGLNDD EIEKMVRDAE ANAEEDRKFE ELVQARNQGD
     AMVHAVRKTL SEAGDKVSDS EKESIEAAIK DLEEALEGSD KEAIEAKTQK LTEVSSELAQ
     KMYADQADQA QQAGGQEEGQ AKSADDAVDA EFEEVKDDDK K