(data stored in ACNUC7421 zone)

SWISSPROT: DNAJ_EDWI9

ID   DNAJ_EDWI9              Reviewed;         377 AA.
AC   C5B7L8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   OrderedLocusNames=NT01EI_0673;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-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.
CC       {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01152};
CC       Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01152};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}.
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. {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01152}.
DR   EMBL; CP001600; ACR67895.1; -; Genomic_DNA.
DR   RefSeq; WP_015870089.1; NC_012779.2.
DR   ProteinModelPortal; C5B7L8; -.
DR   SMR; C5B7L8; -.
DR   STRING; 634503.NT01EI_0673; -.
DR   PRIDE; C5B7L8; -.
DR   EnsemblBacteria; ACR67895; ACR67895; NT01EI_0673.
DR   GeneID; 7962007; -.
DR   KEGG; eic:NT01EI_0673; -.
DR   PATRIC; fig|634503.3.peg.606; -.
DR   eggNOG; ENOG4105BZ5; Bacteria.
DR   eggNOG; COG0484; LUCA.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; DMGGFAD; -.
DR   OrthoDB; POG091H00PT; -.
DR   Proteomes; UP000001485; Chromosome.
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   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; -; 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; 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;
DR   PRODOM; C5B7L8.
DR   SWISS-2DPAGE; C5B7L8.
KW   Chaperone; Complete proteome; Cytoplasm; DNA replication;
KW   Metal-binding; Reference proteome; Repeat; Stress response; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    377       Chaperone protein DnaJ.
FT                                /FTId=PRO_1000213681.
FT   DOMAIN        5     70       J. {ECO:0000255|HAMAP-Rule:MF_01152}.
FT   REPEAT      145    152       CXXCXGXG motif.
FT   REPEAT      162    169       CXXCXGXG motif.
FT   REPEAT      184    191       CXXCXGXG motif.
FT   REPEAT      198    205       CXXCXGXG motif.
FT   ZN_FING     132    210       CR-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   COMPBIAS     77    115       Gly-rich.
FT   METAL       145    145       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       148    148       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       162    162       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       165    165       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       184    184       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       187    187       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       198    198       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       201    201       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
SQ   SEQUENCE   377 AA;  41262 MW;  0946C6735DD1FC71 CRC64;
     MAKKDYYEIL GVSREADERE IKKAYKRLAM KYHPDRNQGD KEAEDKFKEI KEAYEILTDA
     QKRAAYDQYG HAAFEQGGMG GGGGGFGGGA DFSDIFGDVF GDIFGGGRRQ RAARGADLRY
     NMDLTLEEAV RGVTKEIRIP TLAECDVCHG SGAKKGSEPI TCPTCHGAGQ VQMRQGFFTV
     QQPCPHCHGR GTIIKDPCNK CHGHGRIEKS KTLSVKIPAG VDTGDRIRLA GEGEAGENGA
     PAGDLYVQVQ VKAHPIFERE DNNLFCEVPI NFAMAALGGE IEVPTLDGRV NLKIPAETQT
     GKMFRMRGRG VKSVRGGAQG DLLCRVVVET PVNLNDKQKQ LLRELEESFG GPASDKNSPR
     SKRFFDGVKK FFDDLTR
//

If you have problems or comments...

PBIL Back to PBIL home page