ID   DNAK_BORPD              Reviewed;         640 AA.
AC   A9IGC3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Bpet1557;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP41896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IGC3; -.
DR   SMR; A9IGC3; -.
DR   STRING; 94624.Bpet1557; -.
DR   PRIDE; A9IGC3; -.
DR   EnsemblBacteria; CAP41896; CAP41896; Bpet1557.
DR   KEGG; bpt:Bpet1557; -.
DR   eggNOG; COG0443; Bacteria.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001225; 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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119675"
FT   REGION          614..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..640
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   640 AA;  69310 MW;  F95D2A039E635838 CRC64;
     MSKIIGIDLG TTNSCVAVMD GGQVKIIENA EGARTTPSIV AYMDDGETLV GAPAKRQAVT
     NPKNTLYAVK RLIGRKFDEK AVQKDIDLMP YSIVKADNGD AWVEARGKKI APPQVSADVL
     RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     LDKSEKGDRK IAVYDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
     IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
     ITRAKLEALV EELIERTIDP CRVAIKDAGV KVSEIDDVIL VGGMTRMPKV QEKVKEFFGK
     DPRKDVNPDE AVAAGAAIQG SVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMIQKNTTIP
     TRFSQTFSTA DDNQPAVTIK VFQGEREIAA GNKSLGEFNL EGIPPAPRGL PQIEVTFDID
     ANGILHVSAK DKGTGKENKI TIKANSGLSE DEIQRMVKDA EANAEEDHRI AELAQTRNQA
     DALVHATRKS LTEYGEKLEA SEKEAIEGAI KELEDVLKDG DKAAIDAKVE ALSTASQKLG
     EKMYADMQAA QAAQQQAADE AKPVDENVVD ADFKEVKRDQ