(data stored in ACNUC7421 zone)

HOGENOM: PROMH_1_PE10

ID   PROMH_1_PE10                         STANDARD;      PRT;   378 AA.
AC   PROMH_1_PE10; B4F2V6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Chaperone protein DnaJ; (PROMH_1.PE10).
GN   Name=dnaJ; OrderedLocusNames=PMI0010;
OS   PROTEUS MIRABILIS HI4320.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROMH_1.PE10.
CC       Proteus mirabilis HI4320 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:DNAJ_PROMH
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   -!- GENE_FAMILY: HOG000226717 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B4F2V6; -.
DR   EMBL; AM942759; CAR40250.1; -; Genomic_DNA.
DR   RefSeq; YP_002149797.1; NC_010554.1.
DR   ProteinModelPortal; B4F2V6; -.
DR   STRING; B4F2V6; -.
DR   GeneID; 6802317; -.
DR   GenomeReviews; AM942759_GR; PMI0010.
DR   OMA; YTMELTL; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   HAMAP; MF_01152; DnaJ; 1; -.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
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.
DR   HOGENOMDNA; PROMH_1.PE10; -.
KW   chaperone protein DnaJ;
KW   Chaperone; Complete proteome; Cytoplasm; DNA replication;
KW   Metal-binding; Repeat; Stress response; Zinc; Zinc-finger.
SQ   SEQUENCE   378 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKRDFYEVL GLSKTADEKE IKRAYKRLAM KYHPDRNQGD KDSESKFKEI KEAYEVLSDP
     QKRAAYDQYG HAAFEQGGFG GQGGGGFGGA DFSDIFGDVF GDIFGGGRRQ QRAARGSDLQ
     YNMDLTLEEA VRGITKEIRI PTLETCDKCH GSGAKEGTSA ETCSTCHGAG QVHLRQGFFT
     VQQPCPTCHG RGKVIKEPCS KCHGDGRVER YKTLSVKIPA GVDTGDRIRL SGEGEAGEQG
     APAGDLYVQV HVRQHHIFER DGNNLYCEVP INFAVAALGG EIEVPTLDGR VKLKIPAETQ
     TGKMFRMKGK GVKSVRSHGV GDLMCRVVVE TPVKLNEKQK QLMEQLGESF GGKGGEKNTP
     RSKSFLDGVK KFFDDLTK
//

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