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DNAK_PARD8
ID   DNAK_PARD8              Reviewed;         643 AA.
AC   A6LDG8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=BDI_1997;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43732.1; -; Genomic_DNA.
DR   RefSeq; WP_005864708.1; NC_009615.1.
DR   AlphaFoldDB; A6LDG8; -.
DR   SMR; A6LDG8; -.
DR   STRING; 435591.BDI_1997; -.
DR   PRIDE; A6LDG8; -.
DR   EnsemblBacteria; ABR43732; ABR43732; BDI_1997.
DR   GeneID; 57234879; -.
DR   KEGG; pdi:BDI_1997; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; PDIS435591:G1G5A-2050-MON; -.
DR   Proteomes; UP000000566; 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; 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   Reference proteome; Stress response.
FT   CHAIN           1..643
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059622"
FT   REGION          599..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   643 AA;  69035 MW;  2A43FF6AB4ABD2AE CRC64;
     MGKIIGIDLG TTNSCVAVLE GNEPVVIANS EGKRTTPSIV AFVEGGERKV GDPAKRQAIT
     NPEKTIFSIK RFMGETYDQV QKEINRVPYK VVRGDNNTPR VDIEGRLYTP QEISAMILQK
     MKKTAEDYLG QEVTEAVITV PAYFSDAQRQ ATKEAGEIAG LTVRRIVNEP TAASLAYGLD
     KTNKDMKIAV FDLGGGTFDI SILELGDGVF EVKSTNGDTH LGGDDFDHVI IDWLAEEFER
     EEGVDLRKDP MALQRLKEAA EKAKIELSST TSTEINLPYI MPVNGIPKHL VKTLTRAKFE
     QLADGLIQAC IEPCRQSLKD AGLSTSDIDE VILVGGSTRI PAVQAIVEKF FGKAPSKGVN
     PDEVVAVGAA IQGGVLTGEV KDVLLLDVTP LSLGIETMGG VMTKLIESNT TIPTKKSETF
     TTAVDNQPSV EIHILQGERS LAKDNKSIGR FHLDGIPAAQ RGVPQIEVTF DIDANGILNV
     SAKDKGTGKV QSIRIEASSG LSDDEVKRMK EEAAANAEAD KKEKERIDKL NQADSMIFQT
     EKQLKDLGDK LPADKKAPIE GALNKLKEAH KAQDIAGIDA AMAELNSVFQ AASQEMYNAQ
     GGGAQGGPQA DPNFGGQQAG GNAGSSNNSK DGNVTDVDFE EVK
 
 
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