DNAK_DESVV
ID DNAK_DESVV Reviewed; 636 AA.
AC A1VFG6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Dvul_2166;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=391774;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP4;
RX PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA Stahl D.A.;
RT "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT plasticity.";
RL Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM29182.1; -; Genomic_DNA.
DR RefSeq; WP_010938112.1; NC_008751.1.
DR AlphaFoldDB; A1VFG6; -.
DR SMR; A1VFG6; -.
DR EnsemblBacteria; ABM29182; ABM29182; Dvul_2166.
DR KEGG; dvl:Dvul_2166; -.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000009173; 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..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059550"
FT REGION 597..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..636
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 636 AA; 68659 MW; E95700A198C810D7 CRC64;
MGKIIGIDLG TTNSCVYVME GKDPKCITNP EGGRTTPSVV AFTDKERLVG DIAKRQAVTN
PERTVFAVKR LMGRRGDAPE VGRWKEHSPY RIVAGANGDA AVEVQGRPYS APEISAMILG
KLKADAEAYL GETVTEAVIT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAASLAYGF
DRKANEKIAV FDLGGGTFDI SILEVGDNVV EVRATNGDTF LGGEDFDQRI ISYLVDEFRR
ENGGIDLARD RMALQRLKEA AEKAKKDLST SMETEVNLPF ITADQTGPKH LMMKLSRAKL
EKLVEDLVER TVEPCRKALA DAGLTAAQID EVVLVGGMTR MPLVQKRVSE FFGKEPNRSV
NPDEVVAMGA AIQGGILAGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTRKSQT
FTTAADNQPS VSIHVLQGER PMASDNMTLG RFELTGIPPA MRGVPQIEVS FDIDANGIVN
VAAKDLGTGK EQSIRITASS GLSEDEIQRL VKEAEAHADD DKKKQELIEA RNQADGLIYG
TEKSIRDLGD KLDAALKADI ETKVTALRGL LESEDVDAIK KASDELAQAS HKLAEQLYKQ
QAQAGGPEAG AQPEGDAGAR KQDDDVVDAD YTEVKK