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DNAK_HALHL
ID   DNAK_HALHL              Reviewed;         647 AA.
AC   A1WX31;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Hhal_1476;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) 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; CP000544; ABM62243.1; -; Genomic_DNA.
DR   RefSeq; WP_011814265.1; NC_008789.1.
DR   AlphaFoldDB; A1WX31; -.
DR   SMR; A1WX31; -.
DR   STRING; 349124.Hhal_1476; -.
DR   PRIDE; A1WX31; -.
DR   EnsemblBacteria; ABM62243; ABM62243; Hhal_1476.
DR   KEGG; hha:Hhal_1476; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000647; 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..647
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059575"
FT   REGION          545..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   647 AA;  69957 MW;  CEC7A925D5DDC404 CRC64;
     MGKIIGIDLG TTNSCVAVME GNKTRVIENA EGDRTTPSVV AFAEDGEVLT GAPAKRQSVT
     NPENTIHAVK RLIGRRFDED VVQRDIKEMP YKIVKADNGD AWVEAQGKKM APPEVSARTL
     QKMKSTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
     LDKEGGDKKV AVYDLGGGTF DVSIIEIAEV DGEKQFEVLS TSGDTFLGGE DFDKRIIDYL
     IQEFKKDQGI DLAQDHLALQ RLREAAEKAK VELSSSQQTE INLPYITADQ SGPKHMAIKL
     TRAKLESLVE DLVERTIEPC KTALKDAGLA AGDIQDVILV GGQTRMPKVQ EKVKEYFGQD
     PRKDVNPDEA VAVGAAIQAG VLGGDVKDVL LLDVTPLSLG IETLGGVMTK IIEKNTTIPT
     KGTQTFSTAE DNQTAVTVHV LQGEREMAKD NKSLGRFDLT DIPPSPRGVP QIEVAFDIDA
     NGILNVSAKD KATGKETGIE IKASSGLTED EIERMVKEAE ENAEEDRRQR ELVEARNQAE
     NMIHSTRKSL SDLGEQVGDA EKQEIESAIS ELEQVKDGED KDAIEQKTQE LATKAGELAQ
     KAYQQAGGGD EASADAGAGE TASGEQKEDV VDADFEEVKD EDGNSRK
 
 
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