DNAK_ANOFW
ID DNAK_ANOFW Reviewed; 605 AA.
AC B7GKC8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Aflv_0835;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ33213.1; -; Genomic_DNA.
DR RefSeq; WP_012574503.1; NC_011567.1.
DR AlphaFoldDB; B7GKC8; -.
DR SMR; B7GKC8; -.
DR STRING; 491915.Aflv_0835; -.
DR EnsemblBacteria; ACJ33213; ACJ33213; Aflv_0835.
DR KEGG; afl:Aflv_0835; -.
DR PATRIC; fig|491915.6.peg.855; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000742; 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..605
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119663"
FT REGION 575..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 605 AA; 65862 MW; 5F1BA614652C471E CRC64;
MSKIIGIDLG TTNSCVAVLE GGEPKVIPNP EGGRTTPSVV AFKNGERLVG EVAKRQAITN
PNTIISIKRH MGTDYKVQIE GKEYTPQQIS AMILQYLKSY AEAYLGEPVT RAVITVPAYF
NDAQRQATKD AGRIAGLEVE RIINEPTAAA LAYGLDKMDE DQTILVYDLG GGTFDVSILE
LGDGVFEVKA TAGDNHLGGD DFDQVIIDYL VEEFKKEHGI DLSKDKMALQ RLKDAAEKAK
KELSGVMQTQ ISLPFISANE NGPLHLEMTL TRAKFEELSA HLVERTMGPV RQALKDAGLT
PADIDKVILV GGSTRIPAVQ EAIKKEIGKE PHKGVNPDEV VAIGAAIQGG VIAGDVKDVV
LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQIFTTAA DNQTAVDIHV LQGERPMAAD
NKTLGRFQLT DIPPAPRGVP QIEVTFDIDA NGIVHVRAKD LGTNKEQSIT IKSSSGLSEE
EIQRMIKEAE ENAEADRKRK EEVELRNEAD HLIFTTEKTL KELEGKVDEA DVKKAQEAKD
ALKAALDGKD IEDIRAKKNA LQEVVQQLSV KLYEQAAKQA QAQQSEGKKD DNVVDAEFEE
VKEDK