ID   DNAK_KINRD              Reviewed;         623 AA.
AC   A6WFV7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Krad_4233;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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; CP000750; ABS05696.1; -; Genomic_DNA.
DR   RefSeq; WP_012086009.1; NC_009664.2.
DR   AlphaFoldDB; A6WFV7; -.
DR   SMR; A6WFV7; -.
DR   STRING; 266940.Krad_4233; -.
DR   PRIDE; A6WFV7; -.
DR   EnsemblBacteria; ABS05696; ABS05696; Krad_4233.
DR   KEGG; kra:Krad_4233; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001116; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..623
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079231"
FT   REGION          496..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   623 AA;  66488 MW;  F311643C49D25621 CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVIANA EGGRTTPSVV AFAKNGEVLV GEIAKRQAVT
     NIDRTVRSVK REVGTNWSTT IDDKKYTPQE ISARVLQKLK RDAESYLGEA VTDAVITVPA
     YFNDAQRQAT KEAGEIAGLN VLRIINEPTA AALAYGLEKG KEDELILVFD LGGGTFDVSL
     LEVGKDEDGF STIQVRATSG DNHLGGDDWD QRVVDHLLKK VSSAYGIDLS KDKIAMQRLR
     ESAEQAKKEL STATSTGISL QYLSMSENGP VHLDETLTRA QFEQMTQDLL DRTKKPFHDV
     IRDADVKLAD IHHVVLVGGS TRMPAVTGVV KELLGGKEPN KGVNPDEVVA IGAALQAGVL
     KGERKDVLLI DVTPLSLGIE TKGGIMTKLI ERNTAIPTKR SEVFTTADDN QPSVLIQVFQ
     GERELARDNK PLGTFELTGI APAPRGVPQV EVTFDIDANG IVHVNAKDRG TGKEQSMTIS
     GGSALSKEDI ERMVKDAEQH ANEDKQRREE AEARNQAEGL VYQTEKFVAD NSDKLPEDGK
     AEVQAAVAEL KTALAGTDAA EIKAKSDAVA QASQKLGAAM YAAQAEGGAA GDAGAQAGPD
     FTKPSASDED VVDAEVVDDE KDK