ID   DNAK_ACIAD              Reviewed;         647 AA.
AC   Q6F6N3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=ACIAD3654;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG70284.1; -; Genomic_DNA.
DR   RefSeq; WP_004930151.1; NC_005966.1.
DR   AlphaFoldDB; Q6F6N3; -.
DR   SMR; Q6F6N3; -.
DR   STRING; 62977.ACIAD3654; -.
DR   EnsemblBacteria; CAG70284; CAG70284; ACIAD3654.
DR   GeneID; 45235816; -.
DR   KEGG; aci:ACIAD3654; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; ASP62977:ACIAD_RS16530-MON; -.
DR   Proteomes; UP000000430; 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..647
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225928"
FT   REGION          603..647
FT                   /note="Disordered"
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   647 AA;  69491 MW;  954D393973B09405 CRC64;
     MAKIIGIDLG TTNSCVAVLE GDKVKVIENA EGTRTTPSIV AYKDSEILVG QSAKRQAVTN
     PKNTLFAIKR LIGRRYEDQA VQKDIGLVPY KIIKADNGDA WVEVNDKKLA PQQVSAEILK
     KMKKTAEDYL GETVTEAVIT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAFGM
     DKKEGDRKVA VYDLGGGTFD VSIIEIADLD GDQQIEVLST NGDTFLGGED FDTALIDYLV
     EEFKKEQSVN LKNDPLALQR LKEAAEKAKI ELSSSSSTEI NLPYITADAT GPKHLVINVT
     RAKLEGLVAD LVARTIEPCR IALKDAGLST SDISDVILVG GQSRMPMVQQ KVQEFFGKEP
     RKDVNPDEAV AIGAAIQGAV LSGDKTDVLL LDVTPLTLGI ETMGGVLTPI IEKNTTIPAK
     KSQVFSTAAD NQPAVDISVY QGERKMAQQN KLLGNFQLGD IPPAPRGVPQ IEVSFDINAD
     GILKVSAKDK STGKEQSIQI KANSGLSDAE IEAMIKDAEA NAEEDRKFEE LAKARNEADA
     LVSSSNKAVK DLGDKVTEDE KTAITTAVSE LEAATKENDV EDIKAKTEAL QNILMPITQR
     AYEQAQGAGG AQGFDPNAFQ GGDAGQQQKA DDGVVDAEFT EVKDDKK