DNAK_GEOSW
ID DNAK_GEOSW Reviewed; 609 AA.
AC C5D4U1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-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=GWCH70_2437;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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; CP001638; ACS25133.1; -; Genomic_DNA.
DR RefSeq; WP_015864547.1; NC_012793.1.
DR AlphaFoldDB; C5D4U1; -.
DR SMR; C5D4U1; -.
DR STRING; 471223.GWCH70_2437; -.
DR EnsemblBacteria; ACS25133; ACS25133; GWCH70_2437.
DR KEGG; gwc:GWCH70_2437; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
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 Stress response.
FT CHAIN 1..609
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000205190"
FT REGION 578..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
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 609 AA; 66201 MW; 31FD522CD228533A CRC64;
MSKIIGIDLG TTNSCVAVLE GGEPKVIPNP EGNRTTPSVV AFKNGERLVG EVAKRQAITN
PNTIISIKRH MGTDYKVEIE GKKYTPQEIS AIILQYLKSY AEDYLGEPVT RAVITVPAYF
NDAQRQATKD AGRIAGLEVE RIINEPTAAA LAYGLDKEED QTILVYDLGG GTFDVSILEL
GDGVFEVKAT AGDNHLGGDD FDQVIIDYLV EQFKQEHGID LSKDKMALQR LKDAAEKAKK
ELSGVTQTQI SLPFISANET GPLHLETTLT RAKFEELSAH LVERTMGPVR QALQDAGLTP
SDIDKVILVG GSTRIPAVQE AIKRELGKEP HKGVNPDEVV AIGAAIQGGV IAGEVKDVVL
LDVTPLSLGI ETMGGVFTKL IERNTTIPTS KSQIFTTAAD NQTTVDIHVL QGERPMAADN
KTLGRFQLTD IPPAPRGVPQ IEVTFDIDAN GIVHVRAKDL GTNKEQSITI KSSSGLSEEE
IQRMIKEAEE NAEADRKRKE AAELRNEADQ LVFTTEKTLK EVEGKVDEAE VKKAQEAKDA
LKAALEKNDI DDIRKKKEAL QEIVQQLSIK LYEQAAKQAQ AQQQAGAGGA AKKDENVVDA
EFEEVKDDK