ID   DNAK_ROSDO              Reviewed;         636 AA.
AC   Q16D45;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=RD1_0378;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(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}.
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DR   EMBL; CP000362; ABG30098.1; -; Genomic_DNA.
DR   RefSeq; WP_011566720.1; NZ_FOOO01000001.1.
DR   AlphaFoldDB; Q16D45; -.
DR   SMR; Q16D45; -.
DR   STRING; 375451.RD1_0378; -.
DR   PRIDE; Q16D45; -.
DR   EnsemblBacteria; ABG30098; ABG30098; RD1_0378.
DR   KEGG; rde:RD1_0378; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000007029; 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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059652"
FT   REGION          533..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..627
FT                   /note="Acidic residues"
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   636 AA;  68619 MW;  7E4E98FBAB77199A CRC64;
     MSKVIGIDLG TTNSCIAIMD GSQPRVVENA EGARTTPSIV AFTDDERLVG QPAKRQAVTN
     PDNTIFGVKR LIGRRNDDAA LAKDKKNLPF AVIDGGNGDA WVEAKGEKYS PSQISAFILG
     KMKETAESYL GEDVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKEQTQTIAV YDLGGGTFDV TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VNYLADTFKK
     EHSVDLTQDK MALQRLKEAA EKAKIELSSS SQTEINQPFI SMGSNGQPLH MVMKLTRSKL
     ESLVGDLIKA SLKPCKDALK DAGLSASDID EIVLVGGMTR MPKVVEEVTK FFGKEPHKGV
     NPDEVVAMGA AIQAGVLQGD VKDVVLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQI
     FSTAEDNQNA VTIRVFQGER EMAADNKILG AFNLENIPPA PRGMPQIEVT FDIDANGIVS
     VGAMDKGTGK EQKITIQASG GLSDEDIEKM VKDAEENADA DKARRELIEA KNQAESLIHS
     TEKSLEEHSD KVDPTTVEAI ELAIAALKDE MESENADKIK SGIQNVTEAA MKLGEAIYNA
     SQEENDDVAE PADGPHDDQD DIVDAEFEDL DNDKRA