ID   DNAK_SOLUE              Reviewed;         636 AA.
AC   Q01PM8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, 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=Acid_7484;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(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; CP000473; ABJ88392.1; -; Genomic_DNA.
DR   RefSeq; WP_011689107.1; NC_008536.1.
DR   AlphaFoldDB; Q01PM8; -.
DR   SMR; Q01PM8; -.
DR   STRING; 234267.Acid_7484; -.
DR   PRIDE; Q01PM8; -.
DR   EnsemblBacteria; ABJ88392; ABJ88392; Acid_7484.
DR   KEGG; sus:Acid_7484; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_0; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059673"
FT   REGION          591..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   636 AA;  69301 MW;  403261334D79CD62 CRC64;
     MGKIIGIDLG TTNSCVAVME GGQPTVIANQ EGNRTTPSVV AFTKSGERLV GQVAKRQAIT
     NPENTVFSIK RFMGRRYDEV NEEMKMVPYK VVRGENGDAR VDIMGKKYSP PEISAMILTK
     LKEAAESYLG EKVTQAVITV PAYFNDAQRQ ATKDAGKIAG LDVLRIINEP TAAALAYGLD
     KKKNETIAVY DFGGGTFDIS VLEVGEGVVE VKSTNGDTHL GGDNIDQRVI DWIVSEFKKE
     NGIDLSKDQM ALQRLKEAAE KAKMELSTLL ETEINLPFIT ADATGPKHLQ MRLSRSRFEQ
     MVEDILQRSM GPCKQAMTDA SVTPSQIDEV VLVGGQTRMP RIQTLVRELF QRDPHQGVNP
     DEVVAIGAAV QGGVLGGEVK DVLLLDVTPL SLGIETMGGV FTKLIERNTT IPTRKSEVFS
     TASDNQPSVE IKVYQGERAM ARDNRLLGVF QLGNIPPAPR GVPQIEVTFD IDANGILNVT
     AKDRGTNNEQ KITITSSSGL SKDEVEKMAR DAEANAADDR KLKDTIDARN RADAMVYNVE
     KTLKEHRAKV GEAEAKEIEA ALEETKKTLN ENDAEKINAA VDRLTTASHK LAEAMYKSSS
     QPGAQEAPPT DGQPKPDEKG KDNVVDAEFV DVDDKK