ID   DNAK_RHILE              Reviewed;         638 AA.
AC   O33528;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Rhizobium leguminosarum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8401:PRL1;
RA   Simpkins S.A., Johnston A.W.B., James R.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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; Y14649; CAA74982.1; -; Genomic_DNA.
DR   AlphaFoldDB; O33528; -.
DR   SMR; O33528; -.
DR   STRING; 936136.ARRT01000006_gene5872; -.
DR   PRIDE; O33528; -.
DR   eggNOG; COG0443; Bacteria.
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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078523"
FT   REGION          514..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   638 AA;  68566 MW;  9C02F0B49A33C00F CRC64;
     MAKVIGIDLG TTNSCVAVMD GKDAKVIENA EGARTTPSMV AFSDDGERLV GQPAKRQAVT
     NPTNTLFAVK RLIGRRYEDP TVEKDKHLVP FTIVKGDNGD AWVEANGKGY SPAQISAMIL
     QKMKETAESY LGEKVEKAVI TVPAYFNDAR PGQPRMPAAS LGLEVLRIIN EPTAAALAYG
     LDKKEGKTIA VYDLGGGTFD ISILEIGDGV FEVKSTNGDT FLGGEDFDMR LVEYLVAEFK
     RDNGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADASGPKH LTLKLTRAKL
     ESLVDDLVQR TIAPCKAALK DAGVTAAEID EVVLVGGMSR MPKVQEVVKQ LFGKEPHKGV
     NPDEVVALGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQT
     FSTAEDNQQA VTIRVSQGER EMAADNKLLG QFDLVCLPPS PRGMPQIEVT FDIDANGIVQ
     VSAKDKGTGK EQQIRIQASG GLSDADIEKM VKDAEAHATE DKKRREAVEA RNQAESLIHS
     SEKSLKDYGD KVSEADRTAI SDAIAALKTA SEASEPDADD IKAKTQTLME VSMKLGQAIY
     EAQQAESGAA GMPPPKAGDN VVDADYEEIK DDDRKKSA