DNAK_NAUPA
ID DNAK_NAUPA Reviewed; 626 AA.
AC B9L8Z0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=NAMH_0687;
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; Nautiliaceae;
OC Nautilia.
OX NCBI_TaxID=598659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(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; CP001279; ACM92937.1; -; Genomic_DNA.
DR RefSeq; WP_015901989.1; NC_012115.1.
DR AlphaFoldDB; B9L8Z0; -.
DR SMR; B9L8Z0; -.
DR STRING; 598659.NAMH_0687; -.
DR EnsemblBacteria; ACM92937; ACM92937; NAMH_0687.
DR KEGG; nam:NAMH_0687; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; DKMVLQR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000448; 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; 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; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 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..626
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133157"
FT REGION 595..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 626 AA; 68109 MW; B62D9E2A917B12A0 CRC64;
MGKVIGIDLG TTNSAMAYYD GKDAKIIANK EGRNTTPSVV AFTDKGEVLV GEPAKRQAIT
NPERTIYSVK RIMGMMCNEP KAQEAKKHVQ YKIVDKNGAC AVEVDGKVYT PQEISAKILM
KLKKDAEEFF GEEVTEAVIT VPAYFNDSQR KATQEAGKIA GLNVLRIINE PTAAALAYGL
DKKGEEKILV YDLGGGTFDV TVLEIGDGTF QVLATDGNAF LGGDDFDNRI VDWLISEFKA
ETGIDLSQDK MALQRLKDAA EQAKKELSTK EETEINLPFI TADASGPKHL VKKLTRAKFE
AMIDDLLQET LRHIDTALED AGLSKDEIDE IVMVGGSTRI PKVQELVSNY FNGKKLNKSV
NPDEVVALGA AIQAGVLKGD VKDVLLLDVT PLSLGIETLG GVMTKIIEKG TTIPVKKSQV
FSTAEDNQTA VTIHVLQGEA ELAKDNKSLG QFNLEGIPPA PRGVPQIEVT FDIDANGVLN
VSAKDKTSGK EQKITITGSS TLSEEEIERM VREAEEANRK EKARIEAIKA RNELDAVAYQ
AEKFINDNKD KLGDVSALEA KIKEAKELIE QQSEDKAKIE ALKNEINTEL QNVAQNMAQQ
QQAQGGAQQQ NQNKGGDDDV IDAEVE