DNAK_TROWT
ID DNAK_TROWT Reviewed; 603 AA.
AC P64409; Q83MQ0; Q83N74;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=TWT_750;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44847.1; -; Genomic_DNA.
DR RefSeq; WP_011096699.1; NC_004572.3.
DR AlphaFoldDB; P64409; -.
DR SMR; P64409; -.
DR STRING; 203267.TWT_750; -.
DR EnsemblBacteria; AAO44847; AAO44847; TWT_750.
DR GeneID; 67388543; -.
DR KEGG; twh:TWT_750; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002200; 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; 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..603
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078578"
FT REGION 578..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 603 AA; 65409 MW; 1F413797D7AB9C0F CRC64;
MSRAVGIDLG TTNSVVAVLE GGEPNVIANA EGLRTTPSVV AFSRDGEVLV GDTAKRQAVT
NVDNTISSVK RHIGTDWTKQ IGDKKYTPQE ISARILSKLK RDAEQYLGEK VTDAVITVPA
YFNDAERQAT KEAGEIAGLN VLRIINEPTA AALAYGLDKG KEDELILVFD LGGGTFDVSL
LEVGKDDDFS TIQVRATSGD NRLGGDDWDQ RIIDWLVDDF RKTTGVDLSS DKIAMQRLRE
ASEQAKKELS SATSANIQLP YISLTESGPV NMDTTITRAQ FEKMTEDLLE RTKNPFRDVL
KEAGVSVDKI SHVVLVGGST RMPAVSDLVK RETGKEPNKG VNPDEVVAVG AALQAGVLRG
ERKDVLLIDV TPLSLGIETK GGIMTKLIER NTAIPTKRSE VFTTAEDNQP SVSIQVFQGE
RELTQDNKNL GTFELTGIAP APRGLPQIEV TFDIDANGIV HVSAKDKGTG KEQSMTITGG
SGLSQDEIDR MIKEAEEHAA EDKNRRARVD QKNQAEQMVY TAEKLIGDNA KVNEEAKKEL
QADIDSLKSA IQADDHDLIK AGTDKLLASQ QKFAQSVYET TKDDPKEQVV DAEVVDEDSG
SSK
