ID   DNAK_PARDP              Reviewed;         638 AA.
AC   A1B4E9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Pden_2302;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL70393.1; -; Genomic_DNA.
DR   RefSeq; WP_011748586.1; NC_008686.1.
DR   AlphaFoldDB; A1B4E9; -.
DR   SMR; A1B4E9; -.
DR   STRING; 318586.Pden_2302; -.
DR   PRIDE; A1B4E9; -.
DR   EnsemblBacteria; ABL70393; ABL70393; Pden_2302.
DR   KEGG; pde:Pden_2302; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000361; Chromosome 1.
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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059623"
FT   REGION          603..638
FT                   /note="Disordered"
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   638 AA;  68693 MW;  7B6D977DD100C2D4 CRC64;
     MSKVIGIDLG TTNSCVAIMD GSQPKVIENS EGARTTPSIV AFTDSERLVG QPAKRQAVTN
     PSNTVFAVKR LIGRRTTDAE VEKDKKLVPY AIVDGGNGDA WVEVRGDKYS PSQISAFILQ
     KMKETAESYL GEPVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKDSKTIAV YDLGGGTFDI TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VNYLADEFKK
     EHGVDLTKDK MALQRLKEAA EKAKIELSSS SQTEINQPFI SMDKDSGTPL HMVMKLTRAK
     LESLVGDLIK RTMKPVQDAL KDAGMSKGDI DEIVLVGGMT RMPKVVEEVT AFFGKEPHKG
     VNPDEVVALG AAIQAGVLQG DVKDVVLLDV TPLSLGIETL GGVFTRLIDR NTTIPTKKSQ
     IFSTAEDNQN AVTIRVFQGE REMAADNKLL GQFNLENIPP APRGMPQIEV TFDIDANGIV
     SVSAKDKGTG KEQKITIQAS GGLSDDEIDR MVKDAEANAE ADKQRKELVE AKNQAESLIH
     TTKKSLEEHG DKVDGSTVEA IELAVGALEE ALKSEDAGKI KGGIQNLMDA SMKLGEAIYK
     ASQAEAGTGD AEGEAGPRDV DDEIVDADFE DLGEDKRK