ID   DNAK_HALMA              Reviewed;         635 AA.
AC   Q01100; Q5UXH4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=rrnAC3339;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1624448; DOI=10.1128/jb.174.14.4594-4605.1992;
RA   Gupta R.S., Singh B.;
RT   "Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of
RT   archaebacterial HSP70 to its eubacterial homologs and a model for the
RT   evolution of the HSP70 gene.";
RL   J. Bacteriol. 174:4594-4605(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; M84006; AAA73181.1; -; Genomic_DNA.
DR   EMBL; AY596297; AAV48029.1; -; Genomic_DNA.
DR   PIR; A42988; A42988.
DR   RefSeq; WP_011224743.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q01100; -.
DR   SMR; Q01100; -.
DR   STRING; 272569.rrnAC3339; -.
DR   EnsemblBacteria; AAV48029; AAV48029; rrnAC3339.
DR   GeneID; 40154133; -.
DR   KEGG; hma:rrnAC3339; -.
DR   PATRIC; fig|272569.17.peg.3865; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001169; Chromosome I.
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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078594"
FT   REGION          487..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..635
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        76
FT                   /note="E -> Q (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="E -> K (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="V -> L (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336..338
FT                   /note="KNV -> RTS (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429
FT                   /note="A -> R (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504..505
FT                   /note="ER -> DG (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586..617
FT                   /note="AGGAAGAGPGGAAGPGGAAGPGGAAGGAAEQG -> QAVPRALVRVARPAPG
FT                   ALPDRAAQQAAAEQGA (in Ref. 1; AAA73181)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   635 AA;  68531 MW;  DD6877DB18495E6A CRC64;
     MASNKILGID LGTTNSAFAV MEGGDPEIIV NGEGERTTPS VVAFDDGERL VGKPAKNQAV
     KNPDETIQSI KRHMGEDDYS VELDGEEYTP EQVSAMILQK IKHDAEEYLG DEIEKAVITV
     PAYFNDRQRQ ATKDAGEIAG FEVERIVNEP TAAAMAYGLD DESDQTVLVY DLGGGTFDVS
     ILDLGGGVYE VVATNGDNDL GGDDWDHAII DYLADEFEAE HGIDLRDDRQ ALQRLTEAAE
     EAKIELSSRK ETRINLPFIA TTDDGPLDLE QKITRAKFES LTEDLIERTV GPTEQALADA
     DYTKSDIDEV ILVGGSTRMP QVQDQVEEMT GQEPKKNVNP DEAVALGAAI QAGVLSGDVD
     DIVLLDVTPL SLGVEVKGGL FERLIDKNTT IPTEESKIFT TAQDNQTQVQ IRVFQGEREI
     AEENELLGAF ALSGIPPAPA GTPQIEVSFN IDENGIVNVE AEDKGSGNKE DITIEGGAGL
     SDDQIEEMQQ EAEQHAEEDE QRRERIEARN EAEASVRRAE TLLDENEEEI DEDLQSDIEA
     KIEDVEEVLE DEDATKEDYE AVTETLSEEL QEIGKQMYQD QAQQAAGGAA GAGPGGAAGP
     GGAAGPGGAA GGAAEQGEEY VDADFEDVEE SDEDE