DNAK_BART1
ID DNAK_BART1 Reviewed; 630 AA.
AC A9ILH7;
DT 20-MAY-2008, 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=BT_0065;
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506;
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(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; AM260525; CAK00566.1; -; Genomic_DNA.
DR RefSeq; WP_012230375.1; NC_010161.1.
DR AlphaFoldDB; A9ILH7; -.
DR SMR; A9ILH7; -.
DR STRING; 382640.BT_0065; -.
DR PRIDE; A9ILH7; -.
DR EnsemblBacteria; CAK00566; CAK00566; BT_0065.
DR KEGG; btr:BT_0065; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001592; 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 Stress response.
FT CHAIN 1..630
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079216"
FT REGION 598..630
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 630 AA; 68092 MW; 618BEBEBB00184FF CRC64;
MAKVIGIDLG TTNSCVAVMD GKNAKVIENS EGARTTPSVV AFTDGGERLV GQPAKRQAVT
NPEGTVFAVK RLIGRRFDDP MVEKDKALVP YKIVKGDNGD AWVEEAGKKY SPSQISAMIL
QKMKETAESY LGEKVEQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKKDGKTIA VYDLGGGTFD ISVLEIGDGV FEVKSTNGDT FLGGEDFDMR LVGYFADEFK
KEQGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADQSGPKH LTMKLTRAKF
ESLVDDLVQR TIEPCKAALK DAGLKAGEID EVVLVGGMTR MPKIQQVVQN FFGKDPHKGV
NPDEVVAMGA AIQGGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQV
FSTADDNQSA VTIRVFQGER EMASDNKLLA QFDLVGIPPA PRGIPQIEVT FDIDANGIVN
VSAKDKGTGK EHQIRIQASG GLSDADIEKM VKDAEEHAAE DKKRREGVEA KNQAEALIHS
TEKSLNEYGD KVSVEEKGQI EAAISDLKSA LEGSDTEEVT TKMQKLAEVS MKLGQAMYES
SQAASADTET ETKDDDVVDA DFEEVNDKKK