ID   DNAK_SACD2              Reviewed;         643 AA.
AC   Q21H36;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Sde_2733;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81993.1; -; Genomic_DNA.
DR   RefSeq; WP_011469210.1; NC_007912.1.
DR   AlphaFoldDB; Q21H36; -.
DR   SMR; Q21H36; -.
DR   STRING; 203122.Sde_2733; -.
DR   EnsemblBacteria; ABD81993; ABD81993; Sde_2733.
DR   KEGG; sde:Sde_2733; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001947; 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; 1.
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..643
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059655"
FT   REGION          608..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..643
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   643 AA;  68304 MW;  89BFA3E82D5BA1D0 CRC64;
     MGKIIGIDLG TTNSCVSILE GNKAKVIENS EGDRTTPSIV AFTEDGEILV GQSAKRQAVT
     NPQNTLFAVK RLIGRKFTDD VVQKDISMVP YKIIAADNGD AWVEVKGDKK APPQISAEVL
     KKMKKTAEDY LGETVTEAVI TVPAYFNDSQ RQATKDAGKI AGLDVKRIIN EPTAAALAYG
     MDKSKGDSTI AVYDLGGGTF DISIIEIADV DGEHQFEVLS TNGDTFLGGE DFDLRLIEYL
     AEEFKKTNGI DLHNDPLALQ RLKEAAEKAK IELSSSQQTE VNLPYITADA TGPKHLVVKL
     SRAKLESLVE ELVNRSLEPL KMAIKDAGVS VSDIDDVILV GGQTRMPMVQ AAVAKFFGKE
     PRKDVNPDEA VAMGAAIQGA VLSGDVKDVL LLDVTPLSLG IETMGGVATP LIEKNTTIPT
     KKSQVFSTAD DNQTAVTIHV VQGERKQASQ NKSLGRFDLA DIPPAPRGMP QIEVTFDIDA
     NGILNVSAKD KATGKEQSIV IKASSGLSDD EIEKMVQDAE ANADADRKFE EVVTARNTLE
     GLIHATKKTL EEAGDKATAD EKSAIESAIA EAEEAAKGED KDAMEAATKK LTEASSSLAQ
     KLYAEQGAAG AGAAGAADAA ADQPADDGAV DAEFEEVKED DGK