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DNAK_PHOV8
ID   DNAK_PHOV8              Reviewed;         638 AA.
AC   A6L2X7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BVU_2382;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
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; CP000139; ABR40041.1; -; Genomic_DNA.
DR   RefSeq; WP_005846379.1; NC_009614.1.
DR   AlphaFoldDB; A6L2X7; -.
DR   SMR; A6L2X7; -.
DR   STRING; 435590.BVU_2382; -.
DR   EnsemblBacteria; ABR40041; ABR40041; BVU_2382.
DR   GeneID; 66750931; -.
DR   KEGG; bvu:BVU_2382; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; BVUL435590:G1G59-2477-MON; -.
DR   Proteomes; UP000002861; 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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059511"
FT   REGION          600..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..627
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   638 AA;  68354 MW;  AE24177EBA478768 CRC64;
     MGKIIGIDLG TTNSCVSVFE GNEPVVIANS EGKRTTPSIV AFVDGGERKV GDPAKRQAIT
     NPQRTIFSIK RFMGETWDQV QKETARVPYK VVKGDNNTPR VDIDGRLYTP QEISAMILQK
     MKKTAEDYLG QEVTEAVITV PAYFSDSQRQ ATKEAGQIAG LEVKRIVNEP TAAALAYGLD
     KAHKDMKIAV FDLGGGTFDI SILEFGGGVF EVLSTNGDTH LGGDDFDQVI IDWLVQEFKN
     DEGADLTKDP MAMQRLKEAA EKAKIELSSS TSTEINLPYI MPVDGMPKHL VKTLTRAKFE
     ALAHNLIQAC LEPCKKAMSD AGLSNSDIDE VILVGGSSRI PAVQELVEKF FGKTPSKGVN
     PDEVVAVGAA VQGAVLTDEI KGVVLLDVTP LSMGIETLGG VMTKLIDANT TIPARKSETF
     STAADNQTEV TIHVLQGERP MAAQNKSIGQ FNLTGIAPAR RGVPQIEVTF DIDANGILKV
     SAKDKATGKE QAIRIEASSG LSKEEIEKMK AEAEANAEAD KKEREKIDKL NQADSMIFST
     ENQLKELGDK LPADKKAPIE AALQKLKDAH KAQDLSAIDT AMAELNTAFQ AASAEMYAQS
     GAQGGAQAGP GAGAGQQANQ GSSNNKEDIQ DADFEEVK
 
 
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