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Database: UniProt
Entry: DNAK_TROWT
LinkDB: DNAK_TROWT
Original site: 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   27-MAR-2024, entry version 113.
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; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC   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   GeneID; 67388543; -.
DR   KEGG; twh:TWT_750; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OrthoDB; 9766019at2; -.
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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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
//
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