DNAK_HALMT
ID DNAK_HALMT Reviewed; 625 AA.
AC Q9HHB9; I3R545;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chaperone protein DnaK;
DE AltName: Full=HSP70;
DE AltName: Full=Heat shock 70 kDa protein;
DE AltName: Full=Heat shock protein 70;
GN Name=dnaK; OrderedLocusNames=HFX_1649;
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RA Kazi A.S., Nair C.K.K.;
RT "Organization of the DNAK locus of the archeabacterial halophile, Haloferax
RT mediterranei.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4;
RX PubMed=22843593; DOI=10.1128/jb.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF069527; AAG23115.1; -; Genomic_DNA.
DR EMBL; CP001868; AFK19355.1; -; Genomic_DNA.
DR RefSeq; WP_004056756.1; NZ_CP039139.1.
DR AlphaFoldDB; Q9HHB9; -.
DR SMR; Q9HHB9; -.
DR STRING; 523841.HFX_1649; -.
DR PRIDE; Q9HHB9; -.
DR EnsemblBacteria; AFK19355; AFK19355; HFX_1649.
DR GeneID; 40157007; -.
DR KEGG; hme:HFX_1649; -.
DR eggNOG; arCOG03060; Archaea.
DR HOGENOM; CLU_005965_2_4_2; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 10764at2157; -.
DR Proteomes; UP000006469; 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; 2.
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.
FT CHAIN 1..625
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078595"
FT REGION 463..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 67374 MW; C3CF4BE0E3573B51 CRC64;
MASNKILGID LGTTNSAFAV MEGGDPEIIV NAEGDRTTPS VVAFTDDGER LVGKPAKNQA
IQNPEHTIRS IKRHMGDDGY TVDIEGEEYT PEQISAMILQ KIKRDAEDYL GDEVEKAVIT
VPAYFNDKQR QATKDAGEIA GLEVERIVNE PTAASMAYGL DDESNQTVLV YDLGGGTFDV
SVLDLGGGVY EVVATNGDNE LGGDDWDEAI IDWLATEFKN DHGIDLREDR QALQRLKDAA
EEAKIELSSR KETTINLPFI TATDSGPVHL EYDLTRAKFE SLTKDLIDRT VEPTEQALED
AGYGKDDIDD VILVGGSTRM PQVLDKVEEI LGSEPKKSVN PDEAVALGAA IQGGVLGGEV
DDIVLLDVTP LSLGIEVKGG LFERLIEKNT TIPTEESKIF TTAADNQTTV QVRVFQGERE
MAEDNELLGE FTLSGIPPAP AGTPQIEVGF NIDENGIVNV SAEDKGSGNA ESITIEGGAG
LSDDEIDRMQ REAEQHAEED KERRRAVEAR NEAEGAVQRA ETLLEENEEN VDDELRADIE
AAIEDVEAVL EDDDASTDEL EDVTEDLSKE LQEIGKRMYQ QQAQAQAGGP GGAGGPGGAD
GPGADADPED FVDADADFDD EDDDE