ID DNAJ_ACIET Reviewed; 376 AA.
AC B9MDJ8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=Chaperone protein DnaJ;
GN Name=dnaJ; OrderedLocusNames=Dtpsy_2572;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates actively in the response to hyperosmotic
CC and heat shock by preventing the aggregation of stress-denatured
CC proteins and by disaggregating proteins, also in an autonomous,
CC DnaK-independent fashion. Unfolded proteins bind initially to
CC DnaJ; upon interaction with the DnaJ-bound protein, DnaK
CC hydrolyzes its bound ATP, resulting in the formation of a stable
CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers
CC the release of the substrate protein, thus completing the reaction
CC cycle. Several rounds of ATP-dependent interactions between DnaJ,
CC DnaK and GrpE are required for fully efficient folding. Also
CC involved, together with DnaK and GrpE, in the DNA replication of
CC plasmids through activation of initiation proteins (By
CC similarity).
CC -!- COFACTOR: Binds 2 zinc ions per monomer (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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
CC center 2 is essential for interaction with DnaK and for DnaJ
CC activity (By similarity).
CC -!- SIMILARITY: Belongs to the DnaJ family.
CC -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC -!- SIMILARITY: Contains 1 J domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001392; ACM34007.1; -; Genomic_DNA.
DR RefSeq; YP_002554007.1; NC_011992.1.
DR ProteinModelPortal; B9MDJ8; -.
DR STRING; 535289.Dtpsy_2572; -.
DR EnsemblBacteria; ACM34007; ACM34007; Dtpsy_2572.
DR GeneID; 7384241; -.
DR KEGG; dia:Dtpsy_2572; -.
DR PATRIC; 21782279; VBIDiaSp55748_2613.
DR eggNOG; COG0484; -.
DR HOGENOM; HOG000226717; -.
DR KO; K03686; -.
DR OMA; NKCHGEG; -.
DR ProtClustDB; PRK10767; -.
DR BioCyc; AEBR535289:GHOO-2614-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.10.230.10; -; 1.
DR HAMAP; MF_01152; DnaJ; 1; -.
DR InterPro; IPR012724; DnaJ.
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; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; DnaJ_N; 1.
DR SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 1.
DR TIGRFAMs; TIGR02349; DnaJ_bact; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chaperone; Complete proteome; Cytoplasm; DNA replication;
KW Metal-binding; Repeat; Stress response; Zinc; Zinc-finger.
FT CHAIN 1 376 Chaperone protein DnaJ.
FT /FTId=PRO_1000164258.
FT DOMAIN 5 72 J.
FT REPEAT 149 156 CXXCXGXG motif.
FT REPEAT 166 173 CXXCXGXG motif.
FT REPEAT 188 195 CXXCXGXG motif.
FT REPEAT 202 209 CXXCXGXG motif.
FT ZN_FING 136 214 CR-type.
FT COMPBIAS 79 119 Gly-rich.
FT METAL 149 149 Zinc 1 (By similarity).
FT METAL 152 152 Zinc 1 (By similarity).
FT METAL 166 166 Zinc 2 (By similarity).
FT METAL 169 169 Zinc 2 (By similarity).
FT METAL 188 188 Zinc 2 (By similarity).
FT METAL 191 191 Zinc 2 (By similarity).
FT METAL 202 202 Zinc 1 (By similarity).
FT METAL 205 205 Zinc 1 (By similarity).
SQ SEQUENCE 376 AA; 40822 MW; A72458B6E9377A3E CRC64;
MSKRDFYEVL GVPKNASDDE LKKAYRKLAM KYHPDRNQGD AAKPAEEKFK EAKEAYEILS
DAQKRAAYDQ YGHAGVDPNM RGGMGGAEGF GGFAEAFGDI FGDMFGGARG RGGRQVYRGN
DLSYAMDVTL EEAAKGKEAQ IRIPSWESCE TCHGSGAKPG TSAKTCGTCQ GSGTVQMRQG
FFSVQQTCPH CRGTGKIIPE PCTACHGQGR VKKQKTLEVK IPAGIDDGMR IRSTGNGEPG
TNGGPPGDLY IEIRIRKHDI FERDGDDLHC QVPVSFITAA LGGEIEVPTL QGKAAIDIPE
GTQAGKQFRL RGKGIKGVRA SYPGDLYCHI IVETPVKLTE HQRKLLKELD ESLKKGGAKH
SPSTESWTDR LKSFFS
//
