ID   DNAK_CARHZ              Reviewed;         604 AA.
AC   Q3AF08;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=CHY_0415;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB16061.1; -; Genomic_DNA.
DR   RefSeq; WP_011343352.1; NC_007503.1.
DR   AlphaFoldDB; Q3AF08; -.
DR   SMR; Q3AF08; -.
DR   STRING; 246194.CHY_0415; -.
DR   PRIDE; Q3AF08; -.
DR   EnsemblBacteria; ABB16061; ABB16061; CHY_0415.
DR   KEGG; chy:CHY_0415; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_3_0_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002706; 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; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..604
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225948"
FT   REGION          578..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   604 AA;  66112 MW;  529A280014507FFA CRC64;
     MGRIVGIDLG TTNSCIAVME GGEVIVIPNA EGGRTTPSVV AFGKNGERIV GQVAKRQAIT
     NPERTVISIK RHMGTNYRVK IDDKEYTPQE ISAMILQKLK QDAEAYLGEK IEKAVITVPA
     YFTDAQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDKE GEQTILVYDL GGGTFDVSIL
     EIGDGVFEVK ATAGNNRLGG DDFDQRIIDW LVENFKKEHG IDLRNDKMAM QRLKEAAEKA
     KIELSGVLET QINLPFIAAN QNGPLHIDVT LTRAKFNELT ADLVEATMGP TRQALADAGL
     KPEDIDKILL VGGSTRIPAV QEAIRKFFNK EPHKGINPDE CVAIGAAIQA AVLAGEVKDV
     VLLDVTPLSL GIETLGGVFT KLIERNTTIP TSKSQIFTTA ADNQTSVEIH VLQGERPMAA
     DNVSLGRFTL TGIPPAPRGV PQIEVRFDID VNGIVHVSAK DLGTGREQSI TITNTSNLSE
     AEIKRMVEEA ERYAEEDRKR KEEVETRNQA DSLIYQAEKT LKDFKDKANP DLVARVEKAI
     AELREAMNSK DVQLMRAKME ELTKPLYELT SSIYQQSANQ NQTQTGTNTQ GNVYDADYKV
     NDDK