ID   DNAK_HALS3              Reviewed;         629 AA.
AC   B0R3H4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=OE_1737R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP13288.1; -; Genomic_DNA.
DR   RefSeq; WP_010902322.1; NC_010364.1.
DR   AlphaFoldDB; B0R3H4; -.
DR   SMR; B0R3H4; -.
DR   EnsemblBacteria; CAP13288; CAP13288; OE_1737R.
DR   GeneID; 5953701; -.
DR   GeneID; 62886141; -.
DR   KEGG; hsl:OE_1737R; -.
DR   HOGENOM; CLU_005965_2_1_2; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; B0R3H4; -.
DR   Proteomes; UP000001321; 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; 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.
FT   CHAIN           1..629
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119710"
FT   REGION          576..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..629
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  67397 MW;  64D052402A800350 CRC64;
     MASEKILGVD LGTTNSAFAV MEGSDPEIIT NEEGDRTTPS IVAHDDGELL VGKPAKNQAV
     QNPDQTIASI KRHMGEEDYT VALGDDEYTP EEISARILQK IKRDAEEYLG QDVEKAVITV
     PAYFNDRQRQ ATKDAGEIAG FDVERIVNEP TAASMAYGLD EDRDQTVLVY DLGGGTFDVS
     ILDLGGGVYE VAATNGDNDL GGDDWDHAII DHLADNFENE HGIDLREDRQ ALQRLTEAAE
     EAKIELSSRK ETTVNLPFVT ATDSGPVHLE QDITRATFES ITEDLIERTV GPTEQALEDA
     GLSKSDIDDV ILVGGSTRMP QVQAQVEDLV GQEPKKNVNP DEAVALGAAV QGGVLSGEVD
     DIVLVDVTPL SLGIEVKGGL FERLIEKNTA IPTTASKVFT TAADNQTSVQ IRVFQGEREI
     ASENELLGDF HLTGIPPAPA GTPQIEVTFE IDADGIVNVE AEDQGSGNAE SITIEGGAGL
     SDEQIDEMQE DAEAHAEEDE QRRRRIEARN EAETAIQRAE SLLEENEELV DEDLEADVND
     AIDDVQAVLD EDEPEIDALE TATEELSDTL QEIGKQAYQQ QQDAQAGAAG GAGGMGGMGG
     MADGPGGAAD ADGDDEEYVD ADFEDVDEE