DNAK_GEOMG
ID DNAK_GEOMG Reviewed; 638 AA.
AC Q39PT7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Gmet_3532;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) 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; CP000148; ABB33737.1; -; Genomic_DNA.
DR RefSeq; WP_004513688.1; NC_007517.1.
DR AlphaFoldDB; Q39PT7; -.
DR SMR; Q39PT7; -.
DR STRING; 269799.Gmet_3532; -.
DR PRIDE; Q39PT7; -.
DR EnsemblBacteria; ABB33737; ABB33737; Gmet_3532.
DR KEGG; gme:Gmet_3532; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_0_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000007073; 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..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059567"
FT REGION 600..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..638
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 638 AA; 68479 MW; C5392664FD5165D3 CRC64;
MSKVIGIDLG TTNSCVAIME GGEPVVIANS EGSRTTPSMV AFAESGERLV GQQAKRQAVT
NPENTLFAIK RLIGRKFDTD EVRKDISISP FKIVKADNGD AWVDVRGKMY SPPEVSAIVL
QKMKKTAEDY LGETVTDAVI TVPAYFNDSQ RQATKDAGKI AGLNVLRIIN EPTAAALAYG
LDKKKDEKIA VFDLGGGTFD ISILELGDGV FEVKSTNGDT FLGGEDFDQR VIDWIADEFK
KDQGIDLRGD KMALQRLKEA AEKAKCELSS SMETDINLPF ITADATGPKH LTMKLSRAKL
EALCAELLDK LEGPCRTALK DAGLSPSEVD EVILVGGMTR MPAVQKRVQE IFGKAPNKGV
NPDEVVAIGA GIQGGVLRGD VKDVLLLDVT PLSLGIETLG SVMTKLIDKN TTIPCRKSQV
FSTASDNQPA VTIHVLQGER EMASDNKTLG NFELTGIPPA PRGVPQIEVT FDIDANGIVH
VSAKDLGTGK EQSIRITASS GLSKEEIDKM VREAESHAAD DKKKRELIEA RNHADTLAYS
TEKSLKEYGD KIGDDEKKKI EEAVAALKKA MEGDDVDAIK QATDALTQAS HKLAEAVYAK
TQTEGGAQPG AEADGDTGAK GGEKVVDADF EEVKDDKK