ID   DNAK_NATPD              Reviewed;         656 AA.
AC   Q3IUI0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, 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=NP_0218A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-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; CR936257; CAI48200.1; -; Genomic_DNA.
DR   RefSeq; WP_011321839.1; NC_007426.1.
DR   AlphaFoldDB; Q3IUI0; -.
DR   SMR; Q3IUI0; -.
DR   STRING; 348780.NP_0218A; -.
DR   EnsemblBacteria; CAI48200; CAI48200; NP_0218A.
DR   GeneID; 3702669; -.
DR   KEGG; nph:NP_0218A; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 10764at2157; -.
DR   Proteomes; UP000002698; 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; 2.
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; Reference proteome.
FT   CHAIN           1..656
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226036"
FT   REGION          488..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..656
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  69687 MW;  218117DC128BF072 CRC64;
     MASNKILGID LGTTNSAFAV MEGGDPEIIV NSEGERTTPS VVAFTDDGER LVGKPAKNQA
     VQNPEDTIQS IKRHMGEDDY TVEVGDDEYT PEQISAMILQ KIKRDAEEYL GDDIEKAVIT
     VPAYFNDRQR QATKDAGEIA GFEVERIVNE PTAAAMAYGL DDESDQTVLV YDLGGGTFDV
     SILDLGGGVY EVVATNGDND LGGDDWDEAI IDYLADSFEE EHGIDLREDR QALQRLHEAA
     EEAKIELSSR KETNINLPFI AATDEGPLNL EESISRAKFE SLTSDLVERT VGPTEQALDD
     AGYSKGDIDE VILVGGSTRM PMVQEKVEEL TGQEPKKNVN PDEAVGLGAA IQGGVLSGDV
     DDIVLLDVTP LSLGIEVKGG LFERLIDKNT TIPTEASKVF TTAADNQTSV NIRVFQGERE
     IAEENELLGA FQLTGIPPAP AGTPQIEVTF NIDENGIVNV EAEDQGSGNK EDITIEGGVG
     LSDEEIEEMQ EEAEKHAEED EKRRERIEAR NEAESTLQRA ETLLDENEDA VDDDLRADIE
     ASMDDLREVV EDEDADTDEL TEATEALAEA LQEIGKQMYQ QQAGEGGAGA GAGAAGGMGG
     AGPGGMGGAG PGGMGGAGPG GMGGAGPGAG AGQQGDGEEF VDADFEDVDD EDDEDE