ID   DNAK_METMA              Reviewed;         619 AA.
AC   P0CW13; P27094;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=MM_2505;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32201.1; -; Genomic_DNA.
DR   RefSeq; WP_011034423.1; NC_003901.1.
DR   AlphaFoldDB; P0CW13; -.
DR   SMR; P0CW13; -.
DR   STRING; 192952.MM_2505; -.
DR   EnsemblBacteria; AAM32201; AAM32201; MM_2505.
DR   GeneID; 24882230; -.
DR   GeneID; 66135467; -.
DR   KEGG; mma:MM_2505; -.
DR   PATRIC; fig|192952.21.peg.2868; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000595; 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; 1.
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..619
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000408039"
FT   REGION          580..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  66288 MW;  AFF412BEAF957E39 CRC64;
     MAKILGIDLG TTNSCVAVME GGEAVVIPNA EGSRTTPSVV GFSKKGEKLV GQVAKRQAIS
     NPDNTVYSIK RHMGEANYKV TLNGKDYTPQ EISAMILQKL KADAEAYLGE TIKQAVITVP
     AYFNDSQRQA TKDAGAIAGL EVLRIINEPT AASLAYGLDK GDIDQKILVY DLGGGTFDVS
     ILELGGGVFE VKSTSGDTHL GGDDFDQRVI DYLLAEFKKS EGIDLSKDKA VLQRLKDAAE
     KAKIELSGVA NTNINLPFLT VGTDGEPKHM DIDLTRAQFQ KMTEDLLEKT LVSMRRALSD
     AKLTPNDLDK VILVGGATRM PAVVELVENF TGKKPYKNIN PDEAVAIGAA IQAGVLGGEV
     KDVLLLDVTP LTLGIETLGG IATPLIQRNT TIPTKKSQIF STAADNQPSV EIHVLQGERG
     IASENKTLGR FILDGIPPAP RGIPQIEVTF DIDANGILHV SAKDLGTGKQ QSISIQKPGG
     LSDDEIERMV KDAEMHAEED RKRKEEVEIR NNAEALINAA EKTIKEAGDL ATEDQKSKVN
     AAIEDLKKAL EGKDAEDIKA KTEALQESVY PISTAMYQKA QQAQQAAGGE GGAAGTDARG
     PDETVVDADY EVVDDEKRK