DNAK_JANMA
ID DNAK_JANMA Reviewed; 650 AA.
AC A6T226;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=mma_2883;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(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; CP000269; ABR88999.1; -; Genomic_DNA.
DR RefSeq; WP_012080732.1; NC_009659.1.
DR AlphaFoldDB; A6T226; -.
DR SMR; A6T226; -.
DR STRING; 375286.mma_2883; -.
DR EnsemblBacteria; ABR88999; ABR88999; mma_2883.
DR KEGG; mms:mma_2883; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; JSP375286:MMA_RS14960-MON; -.
DR Proteomes; UP000006388; 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..650
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059581"
FT REGION 608..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
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 650 AA; 69842 MW; 192BC3C7DB9A3CB7 CRC64;
MGKIIGIDLG TTNSCVAIME GGKPKVIENS EGARTTPSVI AYQEDGEILV GAPAKRQAVT
NPKNTLYAVK RLIGRKFDEK EVQKDIGMMP YQIVKADNGD AWISVRDKKL AAQQISAEIL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LDKGGKGDRK IAVYDLGGGT FDISIIEIAD VDGEMQFEVL STNGDTFLGG EDFDQRIIDY
IIDEFKKING LDLSKDAIAL QRIKASAERA KIELSSSQQT EINEPYIAMA NGAPVHLNLK
ITRAKLESLV EELISKTIEP CRTAIKDAGV KVSDIDDIIL VGGMTRMPKV QETVKDFFGK
DPRKDVNPDE AVAVGAAIQG SVLSGDRKDL LLLDVTPLSL GIETLGGVMT KMIQKNTTIP
TKFSQVFSTA DDNQPAVTIK VFQGEREMAV GNKALGEFNL EGIPPSARGT PQIEVTFDID
ANGILHVGAK DKATGKENKI TIKANSGLTE EEIQKMVQDA EANAEEDKRL KELAEAHNQG
DALVHSTRKA LTEYGDKLEA GEKEKIEAAI AELEEALKGS DKAAIDEKSA AVTTAAQKLG
EKMYADMQAQ QAAGAAGGDA GAGDAGHSHA DSKPQQDDVV DADFKEVKDK