DNAK_NITEC
ID DNAK_NITEC Reviewed; 647 AA.
AC Q0AIY1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Neut_0412;
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI58690.1; -; Genomic_DNA.
DR RefSeq; WP_011633532.1; NC_008344.1.
DR AlphaFoldDB; Q0AIY1; -.
DR SMR; Q0AIY1; -.
DR STRING; 335283.Neut_0412; -.
DR PRIDE; Q0AIY1; -.
DR EnsemblBacteria; ABI58690; ABI58690; Neut_0412.
DR KEGG; net:Neut_0412; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001966; 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 Stress response.
FT CHAIN 1..647
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059616"
FT REGION 602..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..647
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 647 AA; 69873 MW; 3D33B10BAE260DCF CRC64;
MAKIIGIDLG TTNSCVAVME NNKPKVIENA EGTRTTPSIV AYAEDNEVLV GASAKRQAVT
NPENTLFAIK RLIGRKFDEE VVQKDISVTP YKIVRADNND AWIEVRGRKI APPEVSAQVL
MKMKKTAEDY LGESVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
MDKKEGDRKI AVYDLGGGTF DISIIEIAEI EGEHQFEVLA TNGDTFLGGE DFDSSVISYL
VEEFRKESGI DLKKDMLALQ RLKDAAEKAK IELSSSQQTE VNLPYITADA SGPKHLAVKI
TRAKLESLVE ELIERTAGPC RTALKDAGLS VSDIDDVILV GGQTRMPKVQ DKVKEIFGKE
PRKDVNPDEA VAIGAAIQGG VLQGDVKDVL LLDVTPLSLG IETLGGVMTK LIQKNTTIPT
KAQQIFSTAE DSQTAVTIHV LQGEREMASG NKSLGQFNLT DIPPAQRGMP QIEVTFDIDA
NGILHVSAKD KATGKENKIK IQASSGLSED EIQKMVKDAE THAEEDKKAL ELVNSRNQCD
AMIHSVKKSL TEYGDKLEAD EKSKIEAALK DAEEALKSGD KEAIDAKTQV LTEASHKLAE
KMYAQEQAQA GQQAGPGAGS ASAGQSGEKP VEGEVVDAEF EEVKDKK