ID   DNAK_METBU              Reviewed;         620 AA.
AC   Q12WE6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Mbur_1312;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE52230.1; -; Genomic_DNA.
DR   RefSeq; WP_011499375.1; NC_007955.1.
DR   AlphaFoldDB; Q12WE6; -.
DR   SMR; Q12WE6; -.
DR   STRING; 259564.Mbur_1312; -.
DR   EnsemblBacteria; ABE52230; ABE52230; Mbur_1312.
DR   GeneID; 3998600; -.
DR   KEGG; mbu:Mbur_1312; -.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 10764at2157; -.
DR   Proteomes; UP000001979; 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; 2.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059600"
FT   REGION          579..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  66080 MW;  878526BA27337C1D CRC64;
     MGKILGIDLG TTNSCMAVIE GGKPTVIPNA EGGRTTPSVV GFSKKGDKLV GQVAKRQMIA
     NPGNSVSSIK RHIGEGDYKV NLSGKDYTPQ EVSAMILRKL KDDAEAYLGE TITQTVITVP
     AYFNDSQRQA TKDAGQIAGL EVLRIINEPT AASLAYGLDK EEGDHKILVY DLGGGTFDVS
     ILELGDGVFE VLSTSGNTHL GGDDFDQRIT EFLVEEFKKA EGIDLSNDKA ALQRLNDAAE
     KAKIELSGVA STNVNLPFIT ADSNGQPKHI DIDITRAQFE KMTEDLVAKT LESMKMALSD
     AKLTTKDIDR VLLIGGSTRT PAVYNLVKNF IGKDPYKNIN PDEAVAVGAA IQAGVLSGEV
     HDVLLLDVTP LTMGIETLGG VATPLIERNT TIPVKKSQIF STAADSQPSV EIHILQGERG
     IASANKTLGR FVLDGIPPAP RGLPQIEVTF DIDSNGILHV NAKDLGTGKE QSISIQKPGG
     LSDEEIERMV KDAELHAEED KARKEEVETR NNADSLVNAA ENTLKEAGDV ATNEQKEQIE
     AAIADLKTAL EGEDLEAIKS KTEALQESVY KVSAAMYEKA QKEASAGAEA SEDASGPSST
     GSASDDDVVD ADYEVVDEDK