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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
 
 
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