DNAK_RICBR
ID DNAK_RICBR Reviewed; 631 AA.
AC Q1RHH0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=RBE_1113;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(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; CP000087; ABE05194.1; -; Genomic_DNA.
DR RefSeq; WP_011477772.1; NC_007940.1.
DR AlphaFoldDB; Q1RHH0; -.
DR SMR; Q1RHH0; -.
DR STRING; 336407.RBE_1113; -.
DR EnsemblBacteria; ABE05194; ABE05194; RBE_1113.
DR KEGG; rbe:RBE_1113; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_5; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001951; 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..631
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000277995"
FT REGION 599..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 631 AA; 68206 MW; DCD214938B1BB630 CRC64;
MGKVIGIDLG TTNSCVAVME GKEPKVIENS EGERTTPSII AFANGEKLVG QSAKRQAVTN
PRNTVYAVKR LIGRNFTDPM VKKDQEIVPY NIVKADNGDA WVEVEGKKHS PSQISAFILQ
KMKETAENYL GEKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
DKSASKTIAV YDLGGGTFDV SILEIGDGVF EVKSTNGDTF LGGEDFDTRI LEHLINTFKK
ESGIDLRNDP LALQRLKEAA EKAKKELSSA LTTDINLPYI TADNSGPKHL NIKFTRAELE
KLVDDLIEKT IEPCRKALKD AGLKASDIQE VVLVGGMTRM PKVQEAVEKF FGRALHKGVN
PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPSKKSQVF
STADDNQHAV TIRVFQGERE MAKDNKMLGQ FNLEGIPPAP RGVPQIEVTF DIDANGIVHV
SAKDKASGKE QRVTIQASGG LSDAEIEQMV KDAEKNADED KKHKELIEAK NAADSLIYST
EKTLTDYSDK LSSEDKGGVE EALSALKAVL DSEDASLIKE KTESLTAASM KIGEAMYKAQ
SDAGAAGSAS EENTTSNEKV VDADFEDVEK K