ID   DNAK_NITMS              Reviewed;         636 AA.
AC   A9A135;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Nmar_0096;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX11996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A135; -.
DR   SMR; A9A135; -.
DR   STRING; 436308.Nmar_0096; -.
DR   PRIDE; A9A135; -.
DR   EnsemblBacteria; ABX11996; ABX11996; Nmar_0096.
DR   KEGG; nmr:Nmar_0096; -.
DR   eggNOG; arCOG03060; Archaea.
DR   HOGENOM; CLU_005965_2_4_2; -.
DR   OMA; DKMVLQR; -.
DR   PhylomeDB; A9A135; -.
DR   Proteomes; UP000000792; 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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119735"
FT   REGION          579..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  68165 MW;  32ED580704782935 CRC64;
     MGKVIGIDLG TSNSAAAVMM GGKPTIIPAA EGQTAAGKAF PSVVAFSKEG ELLVGEPARR
     QAVTNPDNTI IAAKRKMGSD YTFKIQDKEY KPQQISSFIL QKIKKDAEAF VGETVEKAVI
     TVPAYFDDNQ RQATKDAGTI AGLDVVRIIN EPTAASLAFG LDKAKEDMKI LVFDFGGGTL
     DVTIMEMGGG VFEVMSTSGD TQLGGTDMDK VLIDYIVDEF KKKEGVDLSQ DTTAMTRIRE
     AAEKAKIELS TVMETDVNLP FIAHDPSSGA KNLELRLTRS KLDELIGPIV DRCKPSIQKA
     LEDAKLSNSD INKIVMIGGP TRIPLVKKFV SEVIGKEVES GVDPMEAVAM GAAIQAGIIA
     GDVTSDIVLL DVTPLTLGIE TLGGVREPLI ERNTTIPTSK GKVFTTAADN QTAVTIHVVQ
     GERPMATDNV SLGSFNLTDL PPAPRGVPQI EVKFDIDANG IINVTAKDLG TQKEAKITIE
     TKTKLSEEEI EKLKEDAEKF SEEDKKKKEK IDLKNEAESY IYTTEKLVNH DLKDKISQEQ
     GIKITDAVKE VKEVLDKEPE ELKPKLEALQ SIVNEVTTEL YKNAAPPPGA DGQQGADGQQ
     GADGQQGADG QQGADGQQGA DGQTTESSSN DETKTN