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Database: UniProt
Entry: DNAK_THIDA
LinkDB: DNAK_THIDA
Original site: DNAK_THIDA 
ID   DNAK_THIDA              Reviewed;         639 AA.
AC   Q3SIN4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=Tbd_1538;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97491.1; -; Genomic_DNA.
DR   RefSeq; WP_011312050.1; NC_007404.1.
DR   AlphaFoldDB; Q3SIN4; -.
DR   SMR; Q3SIN4; -.
DR   STRING; 292415.Tbd_1538; -.
DR   KEGG; tbd:Tbd_1538; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000008291; 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; 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:SF541; CHAPERONE PROTEIN DNAK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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..639
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226024"
FT   REGION          600..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   639 AA;  68996 MW;  7EBDE7CEA719043B CRC64;
     MGRIIGIDLG TTNSCVAVME NGSPKVIENA EGARTTPSIV AYAEDGEILV GAPAKRQAVT
     NPKNTIFAVK RLIGRRFEEK EVQKDIGLMP YKIVKADNGD AWVEVRDKKM AAQQVSAEIL
     RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     MDKKEGDRKI AVYDLGGGTF DISIIEIAEM DGEHQFEVLS TNGDTFLGGE DFDQRLIDYI
     AEEFKKEQGV DLKKDVLALQ RLKEAAEKAK IELSSGQQTE VNLPYITADA SGPKHLAVKI
     TRAKFESLVE ELITRTIEPC KLALKDAGLT TSQIDDVILV GGQTRMPKVM DAVKDFFGKE
     PRRDVNPDEA VAVGAAIQGG VLQGEVKDVL LLDVTPLSLG IETLGGVMTK LIPKNTTIPT
     KASQVFSTAD DNQSAVTVHV LQGEREMASG NKSLGQFNLS DIPPAPRGMP QIEVTFDIDA
     NGILHVSAKD KATGKENKIR IQASSGLSEE EIQRMVKDAE ANAAEDHKAF ELAGARNAAD
     AMIHSVKKSL AEYGDKVSAD EKATIESALK EAEDAVREGD KETIETKTNA LATASHKLAE
     QMYQAEQAKA QPAGETGNQS TGPGNDDVVD AEFEEVKDK
//
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