ID   DNAK_TERTT              Reviewed;         644 AA.
AC   C5BQ33;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=TERTU_3296;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR11735.1; -; Genomic_DNA.
DR   RefSeq; WP_015817846.1; NC_012997.1.
DR   AlphaFoldDB; C5BQ33; -.
DR   SMR; C5BQ33; -.
DR   STRING; 377629.TERTU_3296; -.
DR   EnsemblBacteria; ACR11735; ACR11735; TERTU_3296.
DR   KEGG; ttu:TERTU_3296; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000009080; 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..644
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205199"
FT   REGION          602..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..644
FT                   /note="Basic and acidic 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   644 AA;  68920 MW;  569C7A0E7973D3C4 CRC64;
     MGKIIGIDLG TTNSCVSVLE GDKAKVIENA EGDRTTPSIV AFTDDNEILV GQSAKRQAVT
     NPRNTLFAVK RLIGRKFTDD VVQKDIKMVP YSIVGADNGD AWVEVKGDKK APPQISAEVL
     KKMKKTAEDY LGEKVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
     MDKAKGDRTI AVYDLGGGTF DISVIEIADV DGEHQFEVLS TNGDTFLGGE DFDLRLIEYL
     AEEFKKSNGI DLHNDPLALQ RLKEAAEKAK IELSSSQQTE VNLPYITADA TGPKHLVVKL
     TRAKLESLVE ELVNRSLEPV KMAIKDADLS VSEIDDVILV GGQTRMPLVQ QKVAEFFGKE
     PRKDVNPDEA VAMGAAIQGA VLSGDVKDVL LLDVTPLTLG IETMGGVATP LIEKNTTIPT
     KKSQVFSTAE DNQTAVTIHV VQGERKQAAQ NKSLGRFDLA DIPPAPRGMP QVEVTFDIDA
     NGILNVSAKD KATGKEQSIV IKASSGLSDD EIENMVKDAE ANAEADRKFE ELVSARNTLE
     GLVHATKKTL EEAGDKATAE EKSAIEAAIT EAEEALKSGD KDAIEAATKK VTDASGSLAQ
     KLYAEQSAQQ QGSAGATGGE QPKADKAADD GVVDAEFEEV KDDK