ID   DNAK_RUTMC              Reviewed;         635 AA.
AC   A1AW22;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Rmag_0353;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000488; ABL02129.1; -; Genomic_DNA.
DR   RefSeq; WP_011737754.1; NC_008610.1.
DR   AlphaFoldDB; A1AW22; -.
DR   SMR; A1AW22; -.
DR   STRING; 413404.Rmag_0353; -.
DR   PRIDE; A1AW22; -.
DR   EnsemblBacteria; ABL02129; ABL02129; Rmag_0353.
DR   KEGG; rma:Rmag_0353; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002587; 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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059654"
FT   REGION          595..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   635 AA;  68962 MW;  A2EB28B8899EF332 CRC64;
     MSRIIGIDLG TTNSCVAIMD GGNVKIIENS EGDRTTPSII AYPKDSEEVL VGQPAKRQAV
     TNPENTLYAI KRLIGRRFDE DAVQKDINLV PYKIVKVDNG DAWVEVKGKK MAAPEISAKV
     IGKMKKTAED YLGEEVTEAV ITVPAYFNDS QRQATKDAGK IAGLNVKRII NEPTAAALAY
     GVDKVKGNKT IAVYDLGGGT FDVSIIEMED IDGEKHFEVL STNGDTFLGG EDFDQRIIGY
     LVDEFKRDQG VDLTNDPMAL QRLKEAAEKA KIELSSSEQT DVNLPYVTAD ASGPKHLNIK
     ITRAKLELLV EDLLKRTIEP CKTALKDADL SASDIDEVIL VGGQTRMPKV TKMVQDFFGK
     EPKKDVNPDE AVAMGAAIQA GVLGGDVKDV LLLDVTPLSL GIETMGGIMT KLIEKNTTIP
     TNASQIFSTA VDNQSAVTVH VLQGERNMSS ANKSLGQFNL EGIPNAPKGQ PQVEVTFDID
     SDGILDVSAK DKNTGKEQSI TIKASSGLSD EEVEKMIKDA EAHADEDKKF QELVASKNMA
     DSLIHSTKKT LEELKNEVSD DEKSVIEMAI TELEKAIKND DKKAIDAKIQ TLSKKAQPLT
     EKVQAKSSAE NTSKEKSKAD DDVVDADFEE VKDDK