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DNAK_NITMU
ID   DNAK_NITMU              Reviewed;         644 AA.
AC   Q2Y6U0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Nmul_A2239;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-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; CP000103; ABB75531.1; -; Genomic_DNA.
DR   RefSeq; WP_011381537.1; NZ_FNVK01000006.1.
DR   AlphaFoldDB; Q2Y6U0; -.
DR   SMR; Q2Y6U0; -.
DR   STRING; 323848.Nmul_A2239; -.
DR   PRIDE; Q2Y6U0; -.
DR   EnsemblBacteria; ABB75531; ABB75531; Nmul_A2239.
DR   KEGG; nmu:Nmul_A2239; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002718; 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..644
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059618"
FT   REGION          589..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..644
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   644 AA;  69779 MW;  67D5CC07757E2847 CRC64;
     MGKIIGIDLG TTNSCVAVME SGKPKVIENS EGARTTPSIV AYTEDGEILV GASAKRQAVT
     NPKNTLFAVK RLIGRRFNEE MVQRDIKMVP YTIIKADNND AWIEVRGKKV APPEVSAQVL
     MKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     MDKKEGDRKI AVYDLGGGTF DISIIEIAEV EGEHQFEVLA TNGDTFLGGE DFDARIIEYL
     VDEFKKENGI DLKKDMLALQ RLKDSAEKAK IELSSSQQTE VNLPYITADA SGPKHLAVRI
     TRAKLESLVE DLITRTVEPC RIAIKDAGIK ISDIDDVILV GGQTRMPKVQ EKVKEIFAKE
     PRKDVNPDEA VAVGAAIQGG VLQGAVKDVL LLDVTPLSLG IETLGGVMTK LIQKNTTIPT
     KANQVFSTAD DNQTAVTIHV LQGEREMASG NKSLGQFNLA DIPPAPRGMP QIEVTFDIDS
     NGILHVSAKD KATGKESKIK IQASSGLSEE EVQRMVKDAE AHAEEDHKAM ELVTARNQCD
     AMIHSVQKTM KEHGDKLADE EKSKIESALK EAEDALKSGD KETIEAKTQA LAEASHKLAE
     KMYSQGQGPQ AGPGEEPSGQ SGGTEKPVEG EVVDAEFEEV KNKK
 
 
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