ID   DNAK_METTP              Reviewed;         615 AA.
AC   A0B747;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-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=Mthe_0731;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B747; -.
DR   SMR; A0B747; -.
DR   STRING; 349307.Mthe_0731; -.
DR   PRIDE; A0B747; -.
DR   EnsemblBacteria; ABK14521; ABK14521; Mthe_0731.
DR   KEGG; mtp:Mthe_0731; -.
DR   HOGENOM; CLU_005965_7_0_2; -.
DR   OMA; DKMVLQR; -.
DR   Proteomes; UP000000674; 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; 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..615
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059603"
FT   REGION          579..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  66922 MW;  46A9F6C60F411E75 CRC64;
     MSKIIGIDLG TSNSAAAVLI GGRPTIIPSA EGTSLGGKAF PSYVAFTKDG QVLVGEPARR
     QAITNPEGTI TGIKRKMGTD YKVKVFGKEY TPEEISAHIL RKIKQDAEAF LGEKVEKAVI
     TVPAYFNDNQ RQATKDAGTI AGLDVVRIIN EPTAAALAYG LDKGGEQKIM VFDLGGGTLD
     VTIMEMGEGV FEVKSTSGDT QLGGRDMDER LLDYIVEKFR QETGINLRND VMAMQRLREA
     AEVAKIELSS MLQTTINLPY ITADASGPKH LNMTITRAKL EELIQDVLER CRGPMEQALS
     DAKLSKSDID KIILVGGPTR MPAVQEFVKR VMGKDVERGV DPMECVAMGA AIQAGVLAGE
     VKDILLLDVT PLSLGVETLG GIMTRLIERN TTIPTRKSQI FTTAADNQTS VEIHVLQGER
     PLAKDNISLG RFTLVGIPPA PRGIPQIEVT FDIDANGILH VSAKDLATKK EQRITITAPH
     RLSKEEIEQK VKEAERYAQE DARRREEIET RNQADNLIYT TEKMLKEAGD VATSEQRERI
     EKAISELRDA LSGKDVQEIK SKMEKLQNAV YELSAAMYQR AAQSQSGSAT GSASGSTSGG
     KTVEADYEVV NDDKR