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Database: UniProt
Entry: B9MDJ8
LinkDB: B9MDJ8
Original site: B9MDJ8 
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   19-FEB-2014, entry version 42.
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.
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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; IKDPCNS; -.
DR   OrthoDB; EOG6BPDKP; -.
DR   ProtClustDB; PRK10767; -.
DR   BioCyc; AEBR535289:GHOO-2615-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:UniProtKB-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; PF01556; CTDII; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 3.
DR   SUPFAM; SSF57938; SSF57938; 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
//
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