ID   DNAK_METBF              Reviewed;         620 AA.
AC   Q465Y6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Mbar_A3433;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ72306.1; -; Genomic_DNA.
DR   RefSeq; WP_011308345.1; NC_007355.1.
DR   AlphaFoldDB; Q465Y6; -.
DR   SMR; Q465Y6; -.
DR   STRING; 269797.Mbar_A3433; -.
DR   EnsemblBacteria; AAZ72306; AAZ72306; Mbar_A3433.
DR   GeneID; 3624720; -.
DR   KEGG; mba:Mbar_A3433; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_1_2; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 10764at2157; -.
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.
FT   CHAIN           1..620
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226035"
FT   REGION          577..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  66403 MW;  C029BDCD3D1BB223 CRC64;
     MAKILGIDLG TTNSCMAVME GGEAVVIPNA EGARTTPSVV GFSKKGEKLV GQVAKRQAIS
     NPENTVYSIK RHMGDANYTV TLQGTQYKPQ EISAMILQKL KTDAEAYLGE TIKQAVITVP
     AYFNDAQRQA TKDAGAIAGL DVLRIINEPT SASLAYGLDK GDIEQKILVY DLGGGTFDVS
     ILELGGGVFE VKSTSGDTRL GGDDFDQRIV NYLLAEFRKI EGIDLSKDKA VLQRLTDAAE
     KAKIELSGVA STNINLPFLT VGADGEPKHL DIDLTRAQFQ KMTEDLLEKT LVSMRQALSD
     AKLTPNDLDK VILVGGATRM PAVVELVENF TGKKPYKNIN PDEAVAIGAA IQAGVLGGEV
     KDVLLLDVTP LTLGIETLGG IATPLIPRNT TIPTKKSQVF STAADNQPSV EIHVLQGERG
     VASENKTLGR FTLDGIPPAP RGIPQIEVTF DIDANGILHV GAKDLGTGKE QSISIQKPGG
     LSDDEIDRMV KDAELHAEED KKRKEDVETR NNAEALINAA EKTLKEAGDA ATEDQKSKVT
     AAIDDLKKAL EGKDSEDIKS KTEALQEAVY PISTAMYQKA QQQAQQAQQA EGEAGSHDAQ
     GPDETVVDAD YEVVDDEKRK