DNAK_PSESG
ID DNAK_PSESG Reviewed; 638 AA.
AC Q9WWG9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Pseudomonas savastanoi pv. glycinea (Pseudomonas syringae pv. glycinea).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=318;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PG4180;
RX PubMed=10478477; DOI=10.1094/mpmi.1999.12.7.563;
RA Keith L.M.W., Partridge J.E., Bender C.L.;
RT "dnaK and the heat stress response of Pseudomonas syringae pv. glycinea.";
RL Mol. Plant Microbe Interact. 12:563-574(1999).
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; AF135163; AAD31868.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WWG9; -.
DR SMR; Q9WWG9; -.
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_0000078520"
FT REGION 605..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 638 AA; 68897 MW; DE2C34D28E7FC21B CRC64;
MDRIIGIDLG TTNSCVSILE NGNVKVIENA EGTRTTPSII AYANDGEILV GQSAKRQAVT
NPHNTLYAVK RLIGRKFEED VVQKDIQMVP YKIVKADNGD AWVEVNGQKM APPQISAEIL
KKMKKTAEDY LGEAVTEAVI TVPAYFNDSQ RQATKDAGRI ASVDVKRIIN EPTAAALAYG
MDKAKGDHTV IVYDLGGGTF DVSVIEIAEV DGEHQFEVLA TNGDTFLGGE DFDIRLIDYF
VHEFKKESGM NLKGDPLAMQ RLKEAAEKAK IELSSSTQTE VNLPYITADA TGPKHLVVKI
SRSKLESLVE DLVQRTIAPC EMALKDAGID RSKINDVILV GGQTRMPLVQ KLVTEFFGKE
ARKDVNPDEA VAMGAAIQGA VLAGDVKDVL LLDVSPLTLG IEAMGGVMTA LIKKTPRFLP
RNPSVLTADD NQENAVAIHV LQGERKQAGQ NKSLGKFDLA EIPPAPRGVP QIEVTFDIDA
NGILHVGAKD KATGKQQSIV IKANSGLSEE EIQQMVRDAE VNSEEDRKFE ELASARNQGD
ALVHSTRKMI ADAGDKVTAE QKTAVEAALV ALEAAIKGDD KAAIEAKVEE LSKVSAPIAQ
KMYAEQAENP EAAAKPAEEN AKADDVVDAE FEEVKDHK