ID   DNAK_GRAFK              Reviewed;         641 AA.
AC   A0M353;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=GFO_2083;
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(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; CU207366; CAL67048.1; -; Genomic_DNA.
DR   RefSeq; WP_011709951.1; NC_008571.1.
DR   AlphaFoldDB; A0M353; -.
DR   SMR; A0M353; -.
DR   STRING; 411154.GFO_2083; -.
DR   PRIDE; A0M353; -.
DR   EnsemblBacteria; CAL67048; CAL67048; GFO_2083.
DR   KEGG; gfo:GFO_2083; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_10; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000755; 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   Stress response.
FT   CHAIN           1..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059570"
FT   REGION          596..641
FT                   /note="Disordered"
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   641 AA;  69084 MW;  C183B0DEA429E80D CRC64;
     MSKVIGIDLG TTNSCVAVME GSEPTVIPNA EGKRTTPSVI AFVEGGEIKV GDPAKRQAVT
     NPTKTISSIK RFMGNKYSES SREAGRVPYT VKKGDNDTPR VEIDGRLYTP QELSAMVLQK
     MKKTAEDYLG QDVTEAVITV PAYFNDSQRH ATKEAGEIAG LKVRRIINEP TAAALAYGLD
     KKSQDQKIAV YDLGGGTFDI SILELGDGVF EVLSTNGDTH LGGDDFDEVL IDYLADNFKK
     AEDIDLRKDP MALQRLKEAA EKAKIELSSS SQTEINLPYV TATSSGPKHL VETISRSKFE
     QLAAELVTRS MEPVKKALSD AGLSKSDIDE VILVGGSTRI PKIQEEVEAF FGKKPSKGVN
     PDEVVAIGAA IQGGVLTGDV KDVLLLDVTP LSLGIETMGG VNTKLIESNT TIPTKKSQTF
     STAADNQPSV EIHVLQGERP MATDNKTIGR FHLDGIPPSP RGTPQIEVTF DIDANGIIKV
     SATDKATGKS QDIRIEASSG LTEEEIEKMK KEAEANADAD KQTKEKVDKL NEADAMIFQT
     EKQLKEFGDK ISEDKKKPVE EALEELKKAY ETKELDQITP ALDKINEAWK TASEEMYKAQ
     AEAQGGANGQ PGGPQQGATG AEGGDAKSGD DVEDVDFEEV K