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DNAK_DEIRA
ID   DNAK_DEIRA              Reviewed;         628 AA.
AC   Q9RY23;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 136.
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=DR_0129;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-20.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA   Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT   "Protein recycling is a major component of post-irradiation recovery in
RT   Deinococcus radiodurans strain R1.";
RL   Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
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; AE000513; AAF09718.1; -; Genomic_DNA.
DR   PIR; A75557; A75557.
DR   RefSeq; NP_293855.1; NC_001263.1.
DR   RefSeq; WP_010886777.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RY23; -.
DR   SMR; Q9RY23; -.
DR   STRING; 243230.DR_0129; -.
DR   PRIDE; Q9RY23; -.
DR   EnsemblBacteria; AAF09718; AAF09718; DR_0129.
DR   KEGG; dra:DR_0129; -.
DR   PATRIC; fig|243230.17.peg.293; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   InParanoid; Q9RY23; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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; 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; 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; 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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15249204"
FT   CHAIN           2..628
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078457"
FT   REGION          547..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         195
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   628 AA;  67724 MW;  AC4FCD2EC53759BF CRC64;
     MAKAVGIDLG TTNSVIAVME GGRPEVIVNA EGGRTTPSVV AYKGDEILVG QIARRQAALN
     PAATLFEVKR FIGRRWDEVK EEAARSPFTV KEGPSGSVRI EVNGKDLAPE QVSAEVLRKL
     VSDASAKLGN KITDAVITVP AYFDNSQREA TRQAGEIAGL NVLRVINEPT AAALAYGLER
     KGNETVLVFD LGGGTFDVTI LELGDGVFEV KSTAGDTHLG GADFDYRIVD WLAGEFQKEH
     NFDLRKDKQA LQRLIEAAEK AKIDLSNASE TSISLPFITF DPETRTPMHL ERSLSRAKFE
     ELTADLLRRV RQPVEQALSD AKLSAGDINE VILVGGSTRI PAVKRIVQDL VGKTPNESVN
     PDEAVALGAA VQAGIIQGDS SLGDIVLVDV TPLTLGVEVK GGMIAPMITR NTTVPAKKTE
     IYTTAENNQP GVEINVLQGE RPMAADNKSL GRFKLEGIPP MPAGRAQIEV TFDIDANGIL
     HVTAKEKTSG KESSITIENT TTLDKTDVER MVQEAEQNAA ADKQRKEKVE KRNNLDSLRV
     QAVQQLEEQE GAAQDAKDRL KAAADEAEEA VRSEDDSKIA DAQKKLEEEL RSFMTANQAS
     TQGQPEGTQA QANKADDDVI DADFKPAE
 
 
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