DNAK_ALKHC
ID DNAK_ALKHC Reviewed; 614 AA.
AC Q9KD72;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=BH1346;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; BA000004; BAB05065.1; -; Genomic_DNA.
DR PIR; B83818; B83818.
DR RefSeq; WP_010897512.1; NC_002570.2.
DR AlphaFoldDB; Q9KD72; -.
DR SMR; Q9KD72; -.
DR STRING; 272558.10173962; -.
DR PRIDE; Q9KD72; -.
DR EnsemblBacteria; BAB05065; BAB05065; BAB05065.
DR KEGG; bha:BH1346; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001258; 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; 2.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..614
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078416"
FT REGION 574..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..614
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:0000250"
SQ SEQUENCE 614 AA; 66333 MW; 8A16DCF3115882DD CRC64;
MSKIIGIDLG TTNSCVAVME GGEATVIPNP EGNRTTPSVV AFKDGERQVG EVAKRQAITN
PNTVISIKRH MGTNHKENIE GKEYTPQEIS AIILQKLKSD AEAYLGEEVT KAVITVPAYF
NDSQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKEDD QTILVYDLGG GTFDVSILEL
GDGFFEVKAT SGDNKLGGDD FDQVIIDHLI AEFKKENGID LSQDKMAMQR LKDAAEKAKK
DLSGVTSTQI SLPFITADAT GPKHLELTLT RAKFEELSSH LVERTLGPTR QALQDSGLSA
SEIDKVVLVG GSTRIPAVQE AIKNLTGKEP HKGVNPDEVV ALGAAVQAGV LTGDVKDVVL
LDVTPLSLGI ETMGGVFTKL IERNTTIPTS KSQIFSTAAD NQPSVDIHVL QGEREMAADN
KTLGRFQLTD IPPAPRGVPQ IEVTFDIDAN GIVNVKAKDL GTNKEQSITI TSSSGLTDEE
IDQMVKDAEA NAEADKKRRE EVELRNEADQ LVFTTEKTLK DLGDNVDEAE KTKAEEAKEK
LKKAIEANNI DEIRTAKEEL QQVVQALTTK LYEQAAQQAQ QAQSAEGDQG TAEKGQDDNV
VDADYEEVNE EDKK