DNAK_OLEA2
ID DNAK_OLEA2 Reviewed; 637 AA.
AC Q313S2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Dde_1023;
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB37824.1; -; Genomic_DNA.
DR RefSeq; WP_011367061.1; NC_007519.1.
DR AlphaFoldDB; Q313S2; -.
DR SMR; Q313S2; -.
DR STRING; 207559.Dde_1023; -.
DR EnsemblBacteria; ABB37824; ABB37824; Dde_1023.
DR KEGG; dde:Dde_1023; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; DKMVLQR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002710; 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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225959"
FT REGION 600..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..637
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 637 AA; 68702 MW; 099453836EF04678 CRC64;
MGKIIGIDLG TTNSCVYIME GKDPKCITNP EGGRTTPSVV GFTDKERLVG DIAKRQAVTN
PERTVFAIKR LMGRKADAPE VARWKEHSPY QIVAGPNGDA YVEIEGRKYS PAEVSAMVLA
KLKADAEAYL GETVTEAVIT VPAYFNDSQR QSTKDAGRIA GLDVKRIINE PTAASLAYGF
DKKANEKIAV FDLGGGTFDI SILEVGDNVV EVRATNGDTF LGGEDFDQRV INYLVEEFRR
ENGIDLSRDR MALQRLKEAA EKAKKDLSTS METEINLPFI TADQTGPKHL MIKLSRAKLE
KLVEDLVERT IEPCRKALSD AGLSASEVDE VVLVGGMTRM PLVQKKVADF FGKEPNRSMN
PDEVVSMGAA IQGGILAGDV KDVLLLDVTP LSLGIETLGG VFTRLIERNT TIPTKKSQTF
TTAADNQPSV SIHVMQGERP MASDNMTLGR FELTGIPAAP RGMPQIEVSF DIDANGIVNV
SAKDLGTGKE QSIRITASSG LSEDEIQNLV KEAEAHADED KKKKELIEAR NQADSLIYTT
EKSLSDLGDK LEADLKKEIE DKTAALKTAM EGSDVDAIKK ATDELSQASH KLAEKLYAQQ
QAGAQGAAGA EAGAGDAGAK ASQDEDVVDA DYTEVKN