ID   DNAK_BORA1              Reviewed;         644 AA.
AC   Q2KWA2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=BAV2716;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50327.1; -; Genomic_DNA.
DR   RefSeq; WP_012418358.1; NC_010645.1.
DR   AlphaFoldDB; Q2KWA2; -.
DR   SMR; Q2KWA2; -.
DR   STRING; 360910.BAV2716; -.
DR   PRIDE; Q2KWA2; -.
DR   EnsemblBacteria; CAJ50327; CAJ50327; BAV2716.
DR   GeneID; 41394551; -.
DR   KEGG; bav:BAV2716; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001977; 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..644
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059515"
FT   REGION          609..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..644
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   644 AA;  69818 MW;  B38FA50B54158BEB CRC64;
     MSKIIGIDLG TTNSCVAVMD GGQVKIIENA EGARTTPSIV AYMEDGEILV GAPAKRQAVT
     NPKNTLYAVK RLIGRKFDEK AVQKDIHLMP YTITKADNGD AWVEVRGSKL APPQVSAEVL
     RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     LDKTEKGDRK IAVYDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
     IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
     ITRAKLESLV EELIERTIEP CRVAIKDAGV KVSDIDDVIL VGGMTRMPKV QEKVKEFFGR
     EPRKDVNPDE AVAAGAAIQG SVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMIQKNTTIP
     TRFSQTFSTA DDNQPAVTIK VFQGEREIAA GNKALGEFNL EGIPPAPRGL PQIEVTFDID
     ANGILHVSAK DKGTGKENKI TIKANSGLSE DEIQRMVKDA EANAEEDHRL AELALARNQA
     DALVHATRKS LTEYGDKLEA AEKESIEKAL KDVEESLKAG DKAEIDAKVE ALTQASQKLG
     EKMYADAQAQ QAAQQASHQQ AADNAKPVDD NVVDADFKEV KRDN