DNAK_BARHE
ID DNAK_BARHE Reviewed; 630 AA.
AC Q6G554;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=BH00650;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(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; BX897699; CAF26881.1; -; Genomic_DNA.
DR RefSeq; WP_011180028.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G554; -.
DR SMR; Q6G554; -.
DR STRING; 283166.BH00650; -.
DR PaxDb; Q6G554; -.
DR PRIDE; Q6G554; -.
DR EnsemblBacteria; CAF26881; CAF26881; BH00650.
DR GeneID; 64156373; -.
DR KEGG; bhe:BH00650; -.
DR eggNOG; COG0443; Bacteria.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000421; 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_0000225938"
FT REGION 515..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..532
FT /note="Basic and acidic residues"
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; 68261 MW; B344C9B8B28E5FB1 CRC64;
MAKVIGIDLG TTNSCVAVMD GKNAKVIENS EGARTTPSVV AFTDGGERLV GQPAKRQAVT
NPEGTIFAVK RLIGRRFDDP MVEKDKALVP YKIVKGDNGD AWVEEAGKKY SPSQISAMIL
QKMKETAESY LGEKVEQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKKDGKTIA VYDLGGGTFD ISVLEIGDGV FEVKSTNGDT FLGGEDFDMR LVGYFADEFK
KEQGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADQSGPKH LTMKLTRAKF
ESLVDDLVKR TVEPCKAALK DAGLKAGEID EVVLVGGMTR MPKIQEVVQS FFGKDPHKGV
NPDEVVAMGA AIQGGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQV
FSTADDNQNA VTIRVFQGER EMANDNKLLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVN
VSAKDKGTGK EHQIRIQASG GLSDADIEKM VKDAEEHAAE DKKRREGVEA RNQAEALIHS
TEKSLTEYGD KVSTEEKEQI ETAISDLKSV LDSTDTEEVK AKMQKLAEVS MKLGQAMYEA
SQAATPNTET DTKSDDVVDA DFEEINDKKK