DNAK_HYDCU
ID DNAK_HYDCU Reviewed; 638 AA.
AC Q31HA7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, 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=Tcr_0870;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(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; CP000109; ABB41466.1; -; Genomic_DNA.
DR RefSeq; WP_011370293.1; NC_007520.2.
DR AlphaFoldDB; Q31HA7; -.
DR SMR; Q31HA7; -.
DR STRING; 317025.Tcr_0870; -.
DR PRIDE; Q31HA7; -.
DR EnsemblBacteria; ABB41466; ABB41466; Tcr_0870.
DR KEGG; tcx:Tcr_0870; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
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 Stress response.
FT CHAIN 1..638
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059693"
FT REGION 603..638
FT /note="Disordered"
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 638 AA; 68341 MW; 828F368E68F1757C CRC64;
MGKIIGIDLG TTNSCVAVME GKETKVIPNA EGARTTPSIV AYADDGEVLV GDSAKRQAVT
NPENTLFAIK RLIGRRADDA VVEKDKDMVS YKIIAADNGD AWVQVGDKKL SPQEVSARTL
MKMKKTAEDY LGHEVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
MDKVKADSKI AVYDLGGGTF DISIIEVADL DGEKQVEVLS TNGDTFLGGE DFDNVIVDYI
ATEFKKDQNV DLKLDKLALQ RVREAAEKAK IELSSREQTD INLPYVTADA TGPKHLNMKI
TRAKFESLIE GLVQRSIDPC KTALKDAGLS ASEIDDVILV GGSTRVPMVQ AAVKEFFGKE
PRKDVNPDEA VAMGAAIQGG VLSGDVNDVL LLDVTPLSLG IETMGGVMTK LIEKNTTIPT
RKSQTFSTAE DNQSAVTIHV LQGEREVSSG NKSLGQFNLD EIPPAPRGTP QIEVTFDIDA
NGILNVSAKD KATNKEQHIT IQASSGLSED EIEAMVKDAE AHAAEDAKLK ELVEARNQAD
AMVHGTKKLL DEQGEGVEAA EKEAIEKAIA DLEEAIKGDD KAVIDEKTQA LATASQKLAE
KAYAQPGAEA GAEQQGSANN ADDDIVDAEF EEVNDDKK