ID DNAK_STACT Reviewed; 607 AA.
AC B9DNK0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=Sca_1202;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL28109.1; -; Genomic_DNA.
DR RefSeq; WP_015900449.1; NC_012121.1.
DR AlphaFoldDB; B9DNK0; -.
DR SMR; B9DNK0; -.
DR GeneID; 60545108; -.
DR KEGG; sca:SCA_1202; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OrthoDB; 9766019at2; -.
DR BioCyc; SCAR396513:SCA_RS06020-MONOMER; -.
DR Proteomes; UP000000444; 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 CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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..607
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133160"
FT REGION 489..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..590
FT /note="Polar 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 607 AA; 65852 MW; 093949AFC972C72B CRC64;
MGKIIGIDLG TTNSCVAVLE GDEPKVIQNP EGARTTPSVV AFKNGETQVG EVAKRQAITN
PNTIQSIKRE MGTDYKVDVD GKNYTPQEIS AMILQNLKST AESYLGDKVD KAVITVPAYF
NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTEQ DEKVLVFDLG GGTFDVSILE
LGDGVFEVLS TAGDNKLGGD DFDQVIIDYL VEEFKKENGI DLSQDKMALQ RLKDAAEKAK
KDLSGVSQTQ ISLPFISAGE SGPLHLEITL TRSKFEELSD ELVRRTMGPT RQALSDAGLS
SNDIDEVILV GGSTRIPAVQ EAVKKEVGKE PNKSVNPDEV VAMGAAIQGG VISGDVKDVV
LLDVTPLSLG IEIMGGRMNT LIERNTTIPT SKSQVYSTAA DNQPAVDIHV LQGERPMASD
NKTLGRFSLT DIPPAPRGVP QIEVTFDIDK NGIVNVTAKD LGTNKEQNIT IESSSALSDD
EIDRMVKDAE QNAEEDKKRR EESDLRNEAD SLVFQVDKTL KDLGDNVSED DKKQAEDKKE
ALKSALEGQD LEDIKTKKEE LEKVVQELSM KVYQQAQQGD AAGSNQSDVE DAEYTEVKDD
DDKKDNK
//
