DNAK_PELPD
ID DNAK_PELPD Reviewed; 636 AA.
AC A1ANV0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Ppro_1404;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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; CP000482; ABK99020.1; -; Genomic_DNA.
DR RefSeq; WP_011735313.1; NC_008609.1.
DR AlphaFoldDB; A1ANV0; -.
DR SMR; A1ANV0; -.
DR STRING; 338966.Ppro_1404; -.
DR PRIDE; A1ANV0; -.
DR EnsemblBacteria; ABK99020; ABK99020; Ppro_1404.
DR KEGG; ppd:Ppro_1404; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006732; 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_1000059626"
FT REGION 598..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..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; 68613 MW; 8A242042B445465A CRC64;
MSKVIGIDLG TTNSCVAIME GGEPIVIANS EGSRTTPSIV AFADNGERLV GQQAKRQAVT
NPENTLYAIK RLIGRKFDTE AVKRDIAISP FKIVKADNND AWVEARGKRY SPPEISAFVL
QKMKQTAEDY LGQTVTDAVI TVPAYFDDSQ RQATKDAGKI AGLNVLRIIN EPTAAALAYG
LDKKKEEKVA VFDLGGGTFD ISILELGDGV FEVKSTNGDT FLGGEDFDQL VIDWIADEFH
KDQGINLRGD KMALQRLKEA AEKAKCELSS SMETDINLPF ITADASGPKH LTMKLSRAKL
ETICGELLAK LEGPCRTAMK DAGLSASDID EVILVGGMTR MPAVQKKVEA IFGKTPNRGV
NPDEVVAIGA GIQGGVLKGD VKDVLLLDVT PLSLGIETLG GVMTKLIEKN TTIPCRKSQV
FSTAADNQPA VSIHVLQGER EMSRDNKTLG NFELTGIPPA PRGIPQVEVT FDIDANGIVH
VSAKDLGTGK EQSIRITASS GLSKEEIDKM VRDAESHADE DKKKRDAIEA RNHADSMVYS
TEKSLKEFGD KIDAVEKGNI ENKIVELKKV MDGEDAEAIK KATDELAQAA HKLAEAMYAA
KEQPGEHGET GSGEQARKES GKDENVVDAD FEEVKK