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Database: UniProt
Entry: DNAK_DESVV
LinkDB: DNAK_DESVV
Original site: 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   27-MAR-2024, entry version 94.
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; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
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   KEGG; dvl:Dvul_2166; -.
DR   HOGENOM; CLU_005965_2_1_7; -.
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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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
//
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