DNAK_STAA8
ID DNAK_STAA8 Reviewed; 610 AA.
AC Q2FXZ2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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};
GN OrderedLocusNames=SAOUHSC_01683;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD30757.1; -; Genomic_DNA.
DR RefSeq; WP_000034716.1; NZ_LS483365.1.
DR RefSeq; YP_500193.1; NC_007795.1.
DR AlphaFoldDB; Q2FXZ2; -.
DR SMR; Q2FXZ2; -.
DR STRING; 1280.SAXN108_1606; -.
DR EnsemblBacteria; ABD30757; ABD30757; SAOUHSC_01683.
DR GeneID; 3921795; -.
DR KEGG; sao:SAOUHSC_01683; -.
DR PATRIC; fig|93061.5.peg.1531; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR PRO; PR:Q2FXZ2; -.
DR Proteomes; UP000008816; 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..610
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059677"
FT REGION 525..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
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 610 AA; 66361 MW; B71645C36D26AAED CRC64;
MSKIIGIDLG TTNSCVTVLE GDEPKVIQNP EGSRTTPSVV AFKNGETQVG EVAKRQAITN
PNTVQSIKRH MGTDYKVDIE GKSYTPQEIS AMILQNLKNT AESYLGEKVD KAVITVPAYF
NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTDK DEKVLVFDLG GGTFDVSILE
LGDGVFEVLS TAGDNKLGGD DFDQVIIDYL VAEFKKENGV DLSQDKMALQ RLKDAAEKAK
KDLSGVSQTQ ISLPFISAGE NGPLHLEVNL TRSKFEELSD SLIRRTMEPT RQAMKDAGLT
NSDIDEVILV GGSTRIPAVQ EAVKKEIGKE PNKGVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IEILGGRMNT LIERNTTIPT SKSQIYSTAV DNQPSVDVHV LQGERPMAAD
NKTLGRFQLT DIPPAERGKP QIEVTFDIDK NGIVNVTAKD LGTNKEQRIT IQSSSSLSDE
EIDRMVKDAE VNAEADKKRR EEVDLRNEAD SLVFQVEKTL TDLGENIGEE DKKSAEEKKD
ALKTALEGQD IEDIKSKKEE LEKVIQELSA KVYEQAAQQQ QQAQGANAGQ NNDSTVEDAE
FKEVKDDDKK