DNAK_DESAP
ID DNAK_DESAP Reviewed; 607 AA.
AC B1I699;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Daud_2057;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) 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; CP000860; ACA60547.1; -; Genomic_DNA.
DR RefSeq; WP_012303122.1; NC_010424.1.
DR AlphaFoldDB; B1I699; -.
DR SMR; B1I699; -.
DR STRING; 477974.Daud_2057; -.
DR PRIDE; B1I699; -.
DR EnsemblBacteria; ACA60547; ACA60547; Daud_2057.
DR KEGG; dau:Daud_2057; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008544; 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; 2.
DR Pfam; PF00012; HSP70; 2.
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..607
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119698"
FT REGION 571..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 607 AA; 66089 MW; 4A0531920D8B857E CRC64;
MSKIIGIDLG TTNSCMAVME GGEAVVMPNA EGGRTTPSVV GFSKTGERLV GQVAKRQAIS
NPERTVTSIK RYMGTDHKVR IEGNEYTPQE ISAMILQKMK TDAEAYLGSK VERAVITVPA
YFSDAQRQAT KDAGRIAGLK VERIINEPTA AALAYGLDKE EDQTILVFDL GGGTFDVSIL
ELGDGVFEVK ATSGNNRLGG DDFDQRIIDW IVAEFKKESG IDLSRDRMAM QRLREAAEKA
KVELSSVVNT NINLPFITAD AEGPKHLDLN LSRAKFEELT ADLIEMTMGP TRQAMQDAGL
EPKQIDKILL VGGATRMPSV QEAVRRFFGK EPHKGINPDE CVAIGAAIQA GVLTGEVKDV
VLLDVTPLSL GIETLGGVFT KIIERNTTIP TARSQIFTTA ADNQPSVEIH VLQGERQMAA
GNKTLGRFNL VGIPPAPRGI PQIEVTFDID VNGIVNVSAK DLGTGKSQSI TITGSTGLSD
AEIERMVKEA EQYAEEDRKR REEVEIRNNA DALVYQSEKT LKEHRDQADP NQVSELEQAV
DRLKKALEGG DIERIKRETE NLTGPLHAFT AAMYQKQAQQ QQPGPGPDAG KDKDDKDKTV
DADYEVK