ID   DNAK_RHOS7              Reviewed;         631 AA.
AC   O05700;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
OS   Rhodopseudomonas sp. (strain No.7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas; unclassified Rhodopseudomonas.
OX   NCBI_TaxID=269092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9061015; DOI=10.1016/s0167-4781(96)00222-9;
RA   Momma K., Inui M., Yamagata H., Yukawa H.;
RT   "Cloning of dnaK and dnaJ homologous genes from a purple non-sulfur
RT   bacterium Rhodopseudomonas species.";
RL   Biochim. Biophys. Acta 1350:235-239(1997).
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; D78133; BAA19796.1; -; Genomic_DNA.
DR   AlphaFoldDB; O05700; -.
DR   SMR; O05700; -.
DR   PRIDE; O05700; -.
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   Stress response.
FT   CHAIN           1..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078528"
FT   REGION          517..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   631 AA;  67961 MW;  5D41AAD2779397E7 CRC64;
     MGKVIGIDLG TTNSCVAVMD GKSAKVIENA EGMRTTPSIV AITDDGERLV GQPAKRQAVT
     NPERTFFAVK RLIGRRYDDP MVEKDKGLVP YKIVKASNGD AWVEADGKTY SPSQVSAFIL
     QKMKETAEAH LGQKVDQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     LDKAKTGTIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDMR LVNYLADEFQ
     KEQGIDLRKD KLALQRLKEA AEKAKIELSS TTQTEINLPF ITADQSGPKH LTMKLTRAKF
     EALVDDLVQK TIEPCRKALK DAGLTAGEIS EVVLVGGMTR MPKVQEVVKQ LFGKEPHKGV
     NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRIIDRN TTIPTKKSQV
     FSTAEDNQNA VTIRVFQGER EMAADNKMLG QFDLMGIPPA PRGMPQIEVT FDIDANGIVN
     VSAKDKATGK EQQIRIQASG GLSDSEIDKM VKDAEANAAE DKKRREAVDA KNHADALVHS
     TEKALAEHGS KIDEGERRSI EDALSDLREA LKGDDAEAIK TKSNTLAQAS MKLGEAMYKQ
     AEAGGAAQQA GKDDVVDAEF TEVDDDKKKS A