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DNAK_NOCFA
ID   DNAK_NOCFA              Reviewed;         615 AA.
AC   Q5YNI0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=NFA_54090;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD60261.1; -; Genomic_DNA.
DR   RefSeq; WP_011211943.1; NC_006361.1.
DR   AlphaFoldDB; Q5YNI0; -.
DR   SMR; Q5YNI0; -.
DR   STRING; 247156.NFA_54090; -.
DR   EnsemblBacteria; BAD60261; BAD60261; NFA_54090.
DR   GeneID; 61135979; -.
DR   KEGG; nfa:NFA_54090; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; NFAR247156:NFA_RS26845-MON; -.
DR   Proteomes; UP000006820; 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   Reference proteome; Stress response.
FT   CHAIN           1..615
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225987"
FT   REGION          580..615
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   615 AA;  65760 MW;  65CC72E0E7BA7280 CRC64;
     MARAVGIDLG TTNSVVAVLE GGEPVVVANS EGSRTTPSIV AFAKNGEVLV GQPAKNQAVT
     NVDRTIRSVK RHIGTDWTVE IDGKKYTPQE ISARTLMKLK RDAEAYLGEE ITDAVITVPA
     YFEDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLDKG DKEQTILVFD LGGGTFDVSL
     LEIGEGVVEV RATSGDNHLG GDDWDQRIVN WLVDKFKASS GIDLTKDKMA MQRLREAAEK
     AKIELSSSQS TSINLPYITV DADKNPLFLD EQLSRAEFQK ITSDLLDRTR APFQQVIKDA
     GISVSDIDHV VLVGGSTRMP AVSDLVRELT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
     KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVFQGERE
     IAAHNKLLGS FELTGIPPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTIKIQDGSG
     LSKEEIDRMI KDAEQHAAED KARREEAETR NQAETLVHQT EKFIKDNEDK VPADVKSKVE
     AAIAEANEAL AGTDIAAVKA AVEKLATESQ ALGQAIYEAQ GADAAASSNG AASSANDDQV
     VDAEVVDEPV DTEKK
 
 
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