DNAK_HALSA
ID DNAK_HALSA Reviewed; 629 AA.
AC Q9HRY2; P42372;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=VNG_0491G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7704574; DOI=10.1016/s0960-9822(00)00249-9;
RA Gupta R.S., Singh B.;
RT "Phylogenetic analysis of 70 kD heat shock protein sequences suggests a
RT chimeric origin for the eukaryotic cell nucleus.";
RL Curr. Biol. 4:1104-1114(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 561-629.
RC STRAIN=ATCC 33170 / DSM 669 / NCCB 81095 / NRC 34001;
RX PubMed=9236279; DOI=10.1007/pl00006219;
RA Bustard K., Gupta R.S.;
RT "The sequences of heat shock protein 40 (DnaJ) homologs provide evidence
RT for a close evolutionary relationship between the Deinococcus-thermus group
RT and cyanobacteria.";
RL J. Mol. Evol. 45:193-205(1997).
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; L35530; AAC41461.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19026.1; -; Genomic_DNA.
DR EMBL; U93357; AAB96890.1; -; Genomic_DNA.
DR PIR; F84207; F84207.
DR PIR; T44956; T44956.
DR PIR; T48891; T48891.
DR RefSeq; WP_010902322.1; NC_002607.1.
DR AlphaFoldDB; Q9HRY2; -.
DR SMR; Q9HRY2; -.
DR STRING; 64091.VNG_0491G; -.
DR PaxDb; Q9HRY2; -.
DR EnsemblBacteria; AAG19026; AAG19026; VNG_0491G.
DR GeneID; 5953701; -.
DR GeneID; 62886141; -.
DR KEGG; hal:VNG_0491G; -.
DR PATRIC; fig|64091.14.peg.373; -.
DR HOGENOM; CLU_005965_2_1_2; -.
DR InParanoid; Q9HRY2; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 10764at2157; -.
DR PhylomeDB; Q9HRY2; -.
DR Proteomes; UP000000554; 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; 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..629
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000078596"
FT REGION 576..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 36
FT /note="R -> L (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="D -> G (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="E -> D (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="A -> R (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="E -> K (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="H -> I (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="P -> D (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="G -> A (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 468..469
FT /note="NA -> QR (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 483..484
FT /note="EQ -> DE (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="A -> G (in Ref. 1; AAC41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 584..613
FT /note="AQAGAAGGAGGMGGMGGMADGPGGAADADG -> MPRPARPAALAAWVAWAA
FT WPTARRGGRRRR (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 67397 MW; 64D052402A800350 CRC64;
MASEKILGVD LGTTNSAFAV MEGSDPEIIT NEEGDRTTPS IVAHDDGELL VGKPAKNQAV
QNPDQTIASI KRHMGEEDYT VALGDDEYTP EEISARILQK IKRDAEEYLG QDVEKAVITV
PAYFNDRQRQ ATKDAGEIAG FDVERIVNEP TAASMAYGLD EDRDQTVLVY DLGGGTFDVS
ILDLGGGVYE VAATNGDNDL GGDDWDHAII DHLADNFENE HGIDLREDRQ ALQRLTEAAE
EAKIELSSRK ETTVNLPFVT ATDSGPVHLE QDITRATFES ITEDLIERTV GPTEQALEDA
GLSKSDIDDV ILVGGSTRMP QVQAQVEDLV GQEPKKNVNP DEAVALGAAV QGGVLSGEVD
DIVLVDVTPL SLGIEVKGGL FERLIEKNTA IPTTASKVFT TAADNQTSVQ IRVFQGEREI
ASENELLGDF HLTGIPPAPA GTPQIEVTFE IDADGIVNVE AEDQGSGNAE SITIEGGAGL
SDEQIDEMQE DAEAHAEEDE QRRRRIEARN EAETAIQRAE SLLEENEELV DEDLEADVND
AIDDVQAVLD EDEPEIDALE TATEELSDTL QEIGKQAYQQ QQDAQAGAAG GAGGMGGMGG
MADGPGGAAD ADGDDEEYVD ADFEDVDEE
