ID   DNAK_ELUMP              Reviewed;         619 AA.
AC   B2KAX0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Emin_0100;
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191;
RX   PubMed=19270133; DOI=10.1128/aem.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(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; CP001055; ACC97666.1; -; Genomic_DNA.
DR   RefSeq; WP_012414281.1; NC_010644.1.
DR   AlphaFoldDB; B2KAX0; -.
DR   SMR; B2KAX0; -.
DR   STRING; 445932.Emin_0100; -.
DR   PRIDE; B2KAX0; -.
DR   EnsemblBacteria; ACC97666; ACC97666; Emin_0100.
DR   KEGG; emi:Emin_0100; -.
DR   HOGENOM; CLU_005965_2_4_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001029; 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; 2.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 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..619
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119703"
FT   REGION          584..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         179
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   619 AA;  66365 MW;  C7BB54120B5BEEE1 CRC64;
     MARIIGIDLG TSNTAAAAME GGRATIIPSA EGSSIGGKAF PSYVAFTKDG QRLVGEPARR
     QAIANPEGTV TAFKRRMGED YKFTLRGQEF TPQQLSAFVL QKVKKDAEAF LGEPVEKAVI
     TVPAYFNDNQ RQATKDAGRI AGLEVVRLVN EPTAAALAYG IDKAGKEQKI MVFDLGGGTL
     DVTIMEMGKE GTFDVLSTSG DTKLGGTDMD NAIIEWMVSE FKKSTGIDLS ADKQAAQRLK
     DAAEKAKIEL STTMETDINL PFISAGADGP KHLELKLSRA KLESLVDSIV KRCGASIDQA
     LNDSSLKSTE IDKIILVGGP TRMPIVQKYV EDHAGKKIER GIDPMECVAT GAAVQAGILT
     GDVKDVLLLD VTPLSLGLET LGGVTTRLIE RNTTIPVRKT QVFSTASDNQ PAVTINVLQG
     ERPMAKDNVP LGKFDLDGIP PAPRGVPQIE VTFDIDANGI LNVSAKDLGT NKQQHITITS
     KTKLSDDEVQ KFVKEAEKFA DEDKKTKERV DAKNEADSVL FQTEKALKEH GDKVPQEDRL
     NIDRALGDLK EALKGDDVER IKKAKDDALA ASQKLGEIIY KESQAKAQGA AGPQPGAQAQ
     GQPNDGGKED VVEAEVVDK