DNAK_GEOKA
ID DNAK_GEOKA Reviewed; 607 AA.
AC Q5KWZ7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-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=GK2504;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76789.1; -; Genomic_DNA.
DR RefSeq; WP_011231983.1; NC_006510.1.
DR PDB; 2V7Y; X-ray; 2.37 A; A=1-509.
DR PDB; 4ANI; X-ray; 4.09 A; C/D/G/H=1-509.
DR PDBsum; 2V7Y; -.
DR PDBsum; 4ANI; -.
DR AlphaFoldDB; Q5KWZ7; -.
DR SMR; Q5KWZ7; -.
DR STRING; 235909.GK2504; -.
DR EnsemblBacteria; BAD76789; BAD76789; GK2504.
DR KEGG; gka:GK2504; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR EvolutionaryTrace; Q5KWZ7; -.
DR Proteomes; UP000001172; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..607
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225966"
FT REGION 575..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:2V7Y"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2V7Y"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 86..105
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:2V7Y"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:2V7Y"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:2V7Y"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 386..395
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 404..416
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:2V7Y"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:2V7Y"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 479..490
FT /evidence="ECO:0007829|PDB:2V7Y"
FT HELIX 493..500
FT /evidence="ECO:0007829|PDB:2V7Y"
SQ SEQUENCE 607 AA; 65830 MW; D42D2168CEE358A4 CRC64;
MSKIIGIDLG TTNSCVAVLE GGEVKVIPNP EGNRTTPSVV AFKNGERLVG EVAKRQAITN
PNTIISIKRH MGTDYKVEIE GKQYTPQEIS AIILQYLKSY AEDYLGEPVT RAVITVPAYF
NDAQRQATKD AGRIAGLEVE RIINEPTAAA LAYGLDKEED QTILVYDLGG GTFDVSILEL
GDGVFEVKAT AGDNHLGGDD FDQVIIDYLV NQFKQEHGID LSKDKMALQR LKDAAEKAKK
ELSGVTQTQI SLPFISANEN GPLHLEMTLT RAKFEELSAH LVERTMGPVR QALQDAGLTP
ADIDKVILVG GSTRIPAVQE AIKRELGKEP HKGVNPDEVV AIGAAIQGGV IAGEVKDVVL
LDVTPLSLGI ETMGGVFTKL IERNTTIPTS KSQVFTTAAD NQTTVDIHVL QGERPMAADN
KSLGRFQLTG IPPAPRGVPQ IEVTFDIDAN GIVHVRAKDL GTNKEQSITI KSSSGLSEEE
IQRMIKEAEE NAEADRKRKE AAELRNEADQ LIFMTDKTLK EVEGKVSADE IKKAQDAKEA
LKAALEKNDI DDIRKKKDAL QEAVQQLSIK LYEQAAKQAQ SAGSQGGAAN HKDNVVDAEF
EEVNDDK
