ID   DNAK_DESVM              Reviewed;         639 AA.
AC   B8DRD6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=DvMF_2835;
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19637 / Miyazaki F;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001197; ACL09773.1; -; Genomic_DNA.
DR   RefSeq; WP_015946457.1; NC_011769.1.
DR   AlphaFoldDB; B8DRD6; -.
DR   SMR; B8DRD6; -.
DR   STRING; 883.DvMF_2835; -.
DR   PRIDE; B8DRD6; -.
DR   EnsemblBacteria; ACL09773; ACL09773; DvMF_2835.
DR   KEGG; dvm:DvMF_2835; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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; 2.
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..639
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119700"
FT   REGION          589..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..639
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   639 AA;  68656 MW;  D44EDD9B719AC2D6 CRC64;
     MGKIIGIDLG TTNSCVYVME GKDPKCITNP EGGRTTPSIV AFTDKERLVG DIAKRQAVTN
     PERTVFAVKR LMGRKGDAPE VNNWKTHSPY RIVAGANGDA AVEVQGRQYS AAEVSAMILG
     KLKADAEAYL GETVTDAVIT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAASLAYGF
     DRKTNEKIAV FDLGGGTFDI SILEVGDNVV EVRATNGDTF LGGEDFDQRV INYLVEEFRR
     ENGVDLSKDR MALQRLKEAA EKAKKDLSTS METEINLPFI TADQNGPKHL MMKLSRAKLE
     KLVEDLVDRT IEPCRKALAD AGLSAAQIDE VVLVGGMTRM PLVQKKVGEF FGKEPNRSVN
     PDEVVAMGAA IQGGILAGDV KDVLLLDVTP LSLGIETLGG VFTRLIDRNT TIPTRKSQTF
     TTAADNQPSV SIHVLQGERP MAGDNMTLGR FELSGIPPAM RGTPQVEVTF DIDANGIVNV
     SAKDLGTGKE QSIRITASSG LSESEIQRLI KEAESHADED KKKQELIEAR NQADGLIYGT
     EKSIADLGDK LDAATKSDIE GKIEALKKVM DGSDLEAIKT ASEELSRASH KLAEQLYQQS
     QQGQPGAGPE AGDAGHAGHA GSAKGDDDVV DADYTEVKK