DNAJ_DEIPM
ID DNAJ_DEIPM Reviewed; 310 AA.
AC O34136; F0RMA4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Chaperone protein DnaJ;
GN Name=dnaJ; OrderedLocusNames=Deipr_1909;
OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=693977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM
RC Ac-1939 / CCM 2703 / MRP;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / VKM
RC Ac-1939 / CCM 2703 / MRP;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT 20540.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC heat shock by preventing the aggregation of stress-denatured proteins
CC and by disaggregating proteins, also in an autonomous, DnaK-independent
CC fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC binding to DnaK triggers the release of the substrate protein, thus
CC completing the reaction cycle. Several rounds of ATP-dependent
CC interactions between DnaJ, DnaK and GrpE are required for fully
CC efficient folding. Also involved, together with DnaK and GrpE, in the
CC DNA replication of plasmids through activation of initiation proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
CC ATPase activity. Zinc center 1 plays an important role in the
CC autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2
CC is essential for interaction with DnaK and for DnaJ activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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; U93358; AAB96892.1; -; Genomic_DNA.
DR EMBL; CP002536; ADY27041.1; -; Genomic_DNA.
DR RefSeq; WP_013615649.1; NC_015161.1.
DR AlphaFoldDB; O34136; -.
DR SMR; O34136; -.
DR STRING; 693977.Deipr_1909; -.
DR EnsemblBacteria; ADY27041; ADY27041; Deipr_1909.
DR KEGG; dpt:Deipr_1909; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_0_0; -.
DR OMA; DVNFPET; -.
DR OrthoDB; 1738789at2; -.
DR Proteomes; UP000007718; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; DNA replication; Reference proteome; Repeat;
KW Stress response.
FT CHAIN 1..310
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000070773"
FT DOMAIN 5..70
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 257..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 78..115
FT /note="GGYPGGGFQGGDFGGFDPSQFSDFFQEMFGGRAAGMGG -> ALPRRRLSGR
FT RLRRVRPQPVQRLFPGDVRGPGRWHGS (in Ref. 1; AAB96892)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..148
FT /note="AQGGGR -> LRAEAG (in Ref. 1; AAB96892)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Missing (in Ref. 1; AAB96892)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..264
FT /note="RR -> P (in Ref. 1; AAB96892)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..305
FT /note="QL -> HV (in Ref. 1; AAB96892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 32918 MW; 1A810C9454CE7934 CRC64;
MAYKDYYEVL GVSRSASDSD IKSAYRKLAK QYHPDKNAGD ESAAEKFKEI GEAYAVLSDP
QKRQAYDQFG HTGQVPPGGY PGGGFQGGDF GGFDPSQFSD FFQEMFGGRA AGMGGRGGFT
SPDGRPIDLE DLFGGLGGMG GAAQGGGRRF VQNVEGELQV SLSEAFEGSD EIINVDGRRL
SLRVPAGTRD GARLRLAGQG PGGGDVLLTI RVLEDARFEL DGDDLTTSVD VPAPVAALGG
AVTVQTITGS GQLNVPAGSS GGRRMRLKGQ GWPKKSGGRG DLYVRLNVTV PKELSEEERQ
LYEQLRDLQR
