ID   DNAK_DESAH              Reviewed;         637 AA.
AC   C0QGP6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=HRM2_04030;
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(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; CP001087; ACN13521.1; -; Genomic_DNA.
DR   RefSeq; WP_012662770.1; NC_012108.1.
DR   AlphaFoldDB; C0QGP6; -.
DR   SMR; C0QGP6; -.
DR   STRING; 177437.HRM2_04030; -.
DR   EnsemblBacteria; ACN13521; ACN13521; HRM2_04030.
DR   KEGG; dat:HRM2_04030; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000442; 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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205184"
FT   REGION          597..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   637 AA;  68193 MW;  2D63186FACCA09B7 CRC64;
     MGKIIGIDLG TTNSCVAVME AGEPKVITNS EGNRTTPSVV ALTEGGDRLV GQTAKRQAIT
     NPENTVFGVK RLIGRKFDSP QIQGDKKVLP YKIEASANGD TRINLRGKQH SPAEISSFIL
     ANIKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGKI AGLTVKRIIN EPTAASLAYG
     LDKKGEEKIV VFDLGGGTFD VSVLEIGDGV FEVKSTNGDT HLGGEDFDLR IIDYIADEFK
     KSQGIDIRGD KMALQRLKEA AEKAKMELSS AVETDINLPF ITADASGPKH LDVKLTRAKL
     ESLVADLLDN LVAPCKTALK DAGLTSSDIN EVVLVGGMTR MPAVQERVEK IFSKKPHKGV
     NPDEVVAMGA AIQAGVLQGD VHDVLLLDVT PLSLGIETLG GVMTKLIDKN TTIPTKKSQV
     FSTAADSQPA VSIHVLQGER EMAAGNKTLG QFELTDLPPA PRGVPQIEVT FDIDANGIVH
     VAAKDKATGK EQSIRITAAS GLSEEEIKKM VNDAELHADE DKKKHELVDA KNTAESLIHQ
     TEKTLKEHGD KVDAATKTAI EAACEELKKV KEGTDAAIIK EKSEALTQAS HKLAEAMYQQ
     AAQESGQTEG AAQDPKGAAQ DDDVVDADFE EVKDHKK