ID   DNAK_PICTO              Reviewed;         613 AA.
AC   Q6L0S7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=PTO0840;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43425.1; -; Genomic_DNA.
DR   RefSeq; WP_011177641.1; NC_005877.1.
DR   AlphaFoldDB; Q6L0S7; -.
DR   SMR; Q6L0S7; -.
DR   STRING; 263820.PTO0840; -.
DR   EnsemblBacteria; AAT43425; AAT43425; PTO0840.
DR   GeneID; 2844547; -.
DR   KEGG; pto:PTO0840; -.
DR   PATRIC; fig|263820.9.peg.878; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 10764at2157; -.
DR   Proteomes; UP000000438; 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.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..613
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078601"
FT   REGION          578..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  66352 MW;  9B64E8C5EFC5E7DB CRC64;
     MSKIIGIDLG TSNSAAAVVI SGKPTVIPAA EGVSLGGKAF PSYVAFTKDG QLLVGEPARR
     QALLNPEGTV YAAKRKMGTD YKYKIFGKEY TPQQISAFIL QKIKRDAEAF LGEPVTDAVI
     TVPAYFNDNQ RQATKDAGAI AGLNVRRIIN EPTAACLAYG IDKLNQTLKI VIYDLGGGTL
     DVTIMDFGQG VFQVLSTSGD THLGGTDMDE AIVNFLADNF QRENGIDLRK DHSAYIRLRD
     AAEKAKIELS TVLETEINLP YITATQDGPK HLQYTLTRAK FEELIAPIVD RSKVPLDTAL
     EGAKLKKGDI DKIILIGGPT RIPYVRKYVE DYFGRKAEGG VDPMEAVAMG AAIQGAVLAG
     EVKDIVLLDV TPLTLGIETL GGVMTPLIPA NTTIPTKKSQ IFTTAADMQT TVTIHVVQGE
     RPLAKDDVSL GMFNLDGIPP APRGVPQIEV TFDIDANGIL NVSAKDLGTG KQQSISITAT
     NKLSKDEIER MKKEAEQYAE QDKKAKEEIE TINNAETLAY TAEKTINDAG DKIDESSKES
     VRSIVKDLRD AISSKDINKI KELSEKLTKE IQEIGTKMYQ SQATQGTSQN SSQNNNSQNN
     NGDTVDADFK ESK