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DNAK_RHOE4
ID   DNAK_RHOE4              Reviewed;         617 AA.
AC   C0ZT86;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=RER_13510;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; AP008957; BAH32059.1; -; Genomic_DNA.
DR   RefSeq; WP_019749384.1; NC_012490.1.
DR   AlphaFoldDB; C0ZT86; -.
DR   SMR; C0ZT86; -.
DR   STRING; 234621.RER_13510; -.
DR   EnsemblBacteria; BAH32059; BAH32059; RER_13510.
DR   GeneID; 57488508; -.
DR   KEGG; rer:RER_13510; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002204; Chromosome.
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; 2.
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..617
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205195"
FT   REGION          588..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   617 AA;  66146 MW;  6EF012C33D649E04 CRC64;
     MARAVGIDLG TTNSVVAVLE GGEPVVVANA EGSRTTPSVV AFAKNGEVLV GQPAKNQAVT
     NVDRTLRSVK RHIGTDWNVE IDGKKYTPQE ISARTLMKLK RDAEAYLGED ITDAVITVPA
     YFEDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLDKG DTEQTILVFD LGGGTFDVSL
     LEIGDGVVEV RATSGDNHLG GDDWDERVVA WLVDKFKAQN GIDLTKDKMA LQRLREAAEK
     AKIELSSSQS TSINLPYITV DADKNPLFLD EQLSRSEFQK ITSDLLDRTR APFQAVIKDS
     GIAVKDIDHV VLVGGSTRMP AVSDLVRELT GGREPNKGVN PDEVVAVGAA LQAGVLKGEV
     KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVFQGERE
     IASHNKLLGS FELTDLPPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTIKIQDGSG
     LSKEEIERMV KDAEAHAEED KARREEAEVR NQAESLVHQT EKFVKEQREG ENAGKVSEEI
     LTKVEAAVKD VNDALAGTDI AAVKTAVEKL GTESQALGQA IYEASAANEA GNTDGAGNDD
     DVVDAEVVDE PTDSDKK
 
 
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