DNAK_AZOSB
ID DNAK_AZOSB Reviewed; 641 AA.
AC A1K4C5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=azo1063;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(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; AM406670; CAL93680.1; -; Genomic_DNA.
DR RefSeq; WP_011764797.1; NC_008702.1.
DR AlphaFoldDB; A1K4C5; -.
DR SMR; A1K4C5; -.
DR STRING; 62928.azo1063; -.
DR PRIDE; A1K4C5; -.
DR EnsemblBacteria; CAL93680; CAL93680; azo1063.
DR KEGG; azo:azo1063; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002588; 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..641
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059507"
FT REGION 603..627
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 641 AA; 68761 MW; A2F35BB077BF56FC CRC64;
MGKIIGIDLG TTNSCVSVME GGKPKVIENS EGARTTPSVV AYAEDGEILV GAPAKRQAVT
NARNTLFAVK RLIGRRFEEK EVQKDIDLMP YTIAKADNGD AWVEVRGKKI APPQVSAEVL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
MDKKPGDSKI AVYDLGGGTF DISIIEIADI DGEHQFEVLA TNGDTFLGGE DFDQRIIDYI
VTEFKKEQGV DLKNDVLALQ RLKEAAEKAK IELSSGSQTE VNLPYITADA TGPKHLAIKI
TRAKFESLVE DLIERSIEPC RIALKDAGVK VSDIDDVILV GGQTRMPKVI EKVKEFFGKE
PRRDVNPDEA VAVGASIQGG VLQGEVKDVL LLDVTPLSLG IETLGGVMTK LIQKNTTIPT
KASQVFSTAD DNQSAVTIHV LQGEREMASG NKSLGQFNLS DIPPAPRGMP QIEVTFDIDA
NGILHVSAKD KATGKENKIK IQANSGLSDE EVERMVRDAA AHAEEDKKAH ELVDARNQCD
ALIHSTKKAL AEHGDKIGAD DKAKIEAAMK DAEEAIKSGD KDSIEAKSQA LAMASQKLGE
AMYGQQQAEG GAQAAGAAGG SSKADDADVV DAEFTEVKDK K