ID   DNAK_NITSB              Reviewed;         631 AA.
AC   A6Q421;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=NIS_1121;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       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; AP009178; BAF70230.1; -; Genomic_DNA.
DR   RefSeq; WP_012082493.1; NC_009662.1.
DR   AlphaFoldDB; A6Q421; -.
DR   SMR; A6Q421; -.
DR   STRING; 387092.NIS_1121; -.
DR   EnsemblBacteria; BAF70230; BAF70230; NIS_1121.
DR   KEGG; nis:NIS_1121; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001118; 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; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059619"
FT   REGION          598..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   631 AA;  68470 MW;  E1EF62938705E1ED CRC64;
     MSKVLGIDLG TTNSCMAIYE GKEAKVIPNK EGKNTTPSVV AFTDKGEVLV GDPAKRQMIT
     NPKRTIYSVK RIMGMMCNEE KAQEAKKRLP YNIVDRNGAC AVDVDGKVYT PQEISAKILM
     KLKEDAEAYL GQEITEAVIT VPAYFNDAQR KATKEAGQIA GLNVLRIINE PTAAALAYGL
     DKKEAEKIVV YDLGGGTFDV TILETGDNVV EVLATGGDAF LGGDDFDNRI IDWLVDEFKK
     ETGIDLKSDI MALQRLKEAA ENAKKELSSA METEINLPFI TADQSGPKHL VKKLTRAKFE
     SLIEDLVEKT ITIANNVLKD SGLSKDEVNE VVLVGGSTRI PLVQQKVKEF FGKEPNKSVN
     PDEVVAVGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPVKKSQIF
     STAEDNQPAV TIHVLQGERE MAKDNKSLGQ FTLEGIPPAP RGVPQIEVTF DIDANGILTV
     SAKDKATGKE QKITVTGTSG LSEEEIQRMI QDAEAHKEED RKRKELVETR NQADALAYQT
     EKSLKEVGNA ISADERAQIE AALNDLKNVL KDENATKEQI EAKVQALTQV SHKLAEAMYK
     KEQGQTGGTE QGGTEQKKSG GDDDVIDAEV E