DNAK_EXISA
ID DNAK_EXISA Reviewed; 608 AA.
AC C4L425;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=EAT1b_0616;
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC unclassified Exiguobacterium.
OX NCBI_TaxID=360911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b;
RX PubMed=21460088; DOI=10.1128/jb.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ69547.1; -; Genomic_DNA.
DR RefSeq; WP_012726666.1; NC_012673.1.
DR AlphaFoldDB; C4L425; -.
DR SMR; C4L425; -.
DR STRING; 360911.EAT1b_0616; -.
DR PRIDE; C4L425; -.
DR EnsemblBacteria; ACQ69547; ACQ69547; EAT1b_0616.
DR KEGG; eat:EAT1b_0616; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000716; 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..608
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205188"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 608 AA; 65333 MW; 8C80ED3847211738 CRC64;
MGKIIGIDLG TTNSCVAVME GGEAVVISNA EGNRTTPSVV AFKGEERQVG EVAKRQAITN
PNTIQSIKRH MGTSHTVDVD GKKFTPQEIS AIILQKLKKD AEDYLGESVT EAVITVPAYF
NDAERQATKD AGKIAGLDVK RIINEPTAAA LAYGLDKGED HTILIYDLGG GTFDVSILEL
GDGVFEVVAT AGDNRLGGDD FDQKVIDYLV AEFKKENGID LGKDKMALQR LKDAAEKAKK
DLSGVTSAHI SLPFITAGEA GPLHLEMTLT RAKFEELTAD LVERTMEPTR RALKDAGLTP
SDLDKIILVG GSTRIPAVQK AIHDFTKKEP FKGVNPDEVV ALGAAIQGGV LAGDVKDVVL
LDVTPLSLGI ETMGGVMTKL IDRNTTIPTS KSQVFSTAAD NQPAVDIHVL QGERPMAPDN
KTLGRFQLTD IPPAPRGVPQ IEVKFDIDAN GIVHVSAKDL GTNKEQSITI QSSSGIDEAE
IERMVKEAEA NAEADNKRKE EAELRNETDQ LVFATDKAIK DLGEQVEEAD KEKAEAAKEK
AKTALEGSDL EAIRTAKDEL SAVVQELTQK VYAKMAEQQG AEGAEPQAEA KQDDNVVDAE
FEDLDDRK