DNAK_HALWD
ID DNAK_HALWD Reviewed; 641 AA.
AC Q18GZ4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-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=HQ_2640A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180088; CAJ52751.1; -; Genomic_DNA.
DR RefSeq; WP_011571867.1; NC_008212.1.
DR AlphaFoldDB; Q18GZ4; -.
DR SMR; Q18GZ4; -.
DR STRING; 362976.HQ_2640A; -.
DR EnsemblBacteria; CAJ52751; CAJ52751; HQ_2640A.
DR GeneID; 4193924; -.
DR KEGG; hwa:HQ_2640A; -.
DR eggNOG; arCOG03060; Archaea.
DR HOGENOM; CLU_005965_2_4_2; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001975; 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; 2.
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; Reference proteome.
FT CHAIN 1..641
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059576"
FT REGION 488..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 68791 MW; 2C1B7954F24CED05 CRC64;
MASNKILGID LGTTNSAFAV MEGDDPEIIV NAEGDRTTPS VVAMTDDEER LVGKPAKNQV
IQNPDQTIRS IKRHMGEEDY TVELGGEDYT PEQVSAMILQ KIKRDAEEYL GDEIEKAVIT
VPAYFNDRQR QATKDAGEIA GFEVDRIVNE PTAASMAYGL DDESNQTILV YDLGGGTFDV
SVLDLGGGVY EVVATNGDND LGGDDWDDAV IDWLAGEFED NHGIDLRDDR QALQRLKDAA
EEAKIELSSR KETTINLPFI TATDSGPVHL EETLSRAKFE SLTEDLIERT VGPTEQALED
AGYDDSDIDE VILVGGSTRM PQVREKVEDL LGTEPKKNVN PDEAVALGAA IQGGVLAGDV
DDIVLLDVTP LSLGIEVKGG LFERLIDKNT TIPTEESKVF TTAAANQTSV NVRVFQGERE
IAEENELLGE FQLAGIPPAP AGTPQIEVTF NIDENGIVNV EAEDQGSGNA ESITIEGGAG
LSDEEIEQMQ EEAEAHAEED ERRRERIEAR NSAESAVQRA ETLLEENEED IDDDLKESIE
DEVESVEAVL EDEDATKEEI EDVTESLSSE LQEIGKQMYD AQQAAAGAGA GAAGAGAGAG
PGGMGDMGDM GDMGGAAGSG DADNEYVDAD FEDVDDDTKD E