ID   DNAK_BRADU              Reviewed;         633 AA.
AC   P94317;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=blr0678;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RX   PubMed=9108282; DOI=10.1007/s004380050408;
RA   Minder A.C., Narberhaus F., Babst M., Hennecke H., Fischer H.-M.;
RT   "The dnaKJ operon belongs to the sigma32-dependent class of heat shock
RT   genes in Bradyrhizobium japonicum.";
RL   Mol. Gen. Genet. 254:195-206(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110spc4;
RX   PubMed=10613857; DOI=10.1128/jb.182.1.14-22.2000;
RA   Minder A.C., Fischer H.-M., Hennecke H., Narberhaus F.;
RT   "Role of HrcA and CIRCE in the heat shock regulatory network of
RT   Bradyrhizobium japonicum.";
RL   J. Bacteriol. 182:14-22(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; Y09633; CAA70846.3; -; Genomic_DNA.
DR   EMBL; BA000040; BAC45944.1; -; Genomic_DNA.
DR   RefSeq; NP_767319.1; NC_004463.1.
DR   RefSeq; WP_011083506.1; NZ_CP011360.1.
DR   AlphaFoldDB; P94317; -.
DR   SMR; P94317; -.
DR   STRING; 224911.27348928; -.
DR   PRIDE; P94317; -.
DR   EnsemblBacteria; BAC45944; BAC45944; BAC45944.
DR   GeneID; 64020541; -.
DR   KEGG; bja:blr0678; -.
DR   PATRIC; fig|224911.44.peg.48; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   InParanoid; P94317; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; P94317; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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..633
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078428"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   633 AA;  68293 MW;  DC6F8462CE9C81CB CRC64;
     MGKVIGIDLG TTNSCVAVMD GKNAKVIENS EGMRTTPSIV AVTDDGERLV GQPAKRQAVT
     NPERTFFAVK RLIGRRYDDP MVEKDKKLVP YKIVKASNGD AWVEADGQTY SPSQVSAFIL
     QKMKETAEAH LGQKVDQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKTKTGTIA VYDLGGGTFD ISILEIGDGV FEVKSTNGDT FLGGEDFDMR LVGYLADEFQ
     KEQGINLRND KLALQRLKEA AEKAKIELSS TTQTEINLPF ITADQTGPKH LTMKLTRAKF
     EALVDDLIQK TVEPCRKALK DAGVTAGEIG EVVLVGGMSR MPKVQEVVKQ LFGKEPHKGV
     NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRIIDRN TTIPTKKSQV
     FSTAEDNQNA VTIRVFQGER EMAADNKMLG QFDLMGIPPA PRGMPQIEVT FDIDANGIVN
     VSAKDKATGK EQQIRIQASG GLSEADIEKM VKDAEANAEA DKKRREAVTA KNEADGLVHS
     TEKALAEHGS KVAETERRAI EDAVSDLKEA LKGDDAEAIK AKTQTLAQAS MKLGEAMYKQ
     QAEADAKKDA AKDDVVDAEF TEVDDDKNNK KSA