DNAK_GEODF
ID DNAK_GEODF Reviewed; 636 AA.
AC B9M357;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Geob_1107;
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM19467.1; -; Genomic_DNA.
DR RefSeq; WP_012646196.1; NC_011979.1.
DR AlphaFoldDB; B9M357; -.
DR SMR; B9M357; -.
DR STRING; 316067.Geob_1107; -.
DR PRIDE; B9M357; -.
DR EnsemblBacteria; ACM19467; ACM19467; Geob_1107.
DR KEGG; geo:Geob_1107; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000007721; 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..636
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133145"
FT REGION 602..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 636 AA; 68345 MW; 8CF57AEFA9730CB2 CRC64;
MSKVIGIDLG TTNSCVAIME GGEPIVIANA EGSRTTPSMV AITDSGERLV GQQAKRQAVT
NPENTLFAIK RLIGRKFESE AVKKDIAISP FKIVKADNAD AWVEVRGQKY SPPEISAMVL
QKMKKTAEDY LGETVTDAVI TVPAYFDDSQ RQATKDAGKI AGLNVLRIIN EPTAAALAYG
LDKKKDEKIA VFDLGGGTFD ISILELGEGV FEVKSTNGDT FLGGEDFDQN VIDWIADEFK
KDQGIDLRND KMALQRLKEA AEKAKCELSS SMETDINLPF ITADASGPKH LNLKLTRAKL
EAICANLIDK LEGPCRTALK DAGLSPSDID EVILVGGMTR MPIVQKRVQD IFGKVPNRGV
NPDEVVAIGA AIQGGVLKGD VKDVLLLDVT PLSLGIETLG GVMTRLIEKN STIPCRKSQI
FSTAADNQPA VSIHVLQGER EMAGDNKTLG NFELTGIPAA PRGVPQIEVT FDIDANGIVH
VSAKDLGTGK EQSIRITASS GLSKEEIDKM VREAESHASE DKKKRELIEA RNQADSLVYS
TEKSLSEFGD KIDAAEKQKI EEGLAALKKA MEGNDADAIK KASDELMQAS HKLAEAVYAK
AQPAGEEQAG AAAHEGEAKG EKVVDADFEE VKEDKK