(data stored in ACNUC7421 zone)

SWISSPROT: A8LDT3_FRASN

ID   A8LDT3_FRASN            Unreviewed;       393 AA.
AC   A8LDT3;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN   OrderedLocusNames=Franean1_0231 {ECO:0000313|EMBL:ABW09698.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09698.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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:0000256|HAMAP-Rule:MF_01152}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01152};
CC       Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_01152};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01152}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01152}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01152}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01152}.
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DR   EMBL; CP000820; ABW09698.1; -; Genomic_DNA.
DR   RefSeq; WP_012157675.1; NC_009921.1.
DR   STRING; 298653.Franean1_0231; -.
DR   EnsemblBacteria; ABW09698; ABW09698; Franean1_0231.
DR   KEGG; fre:Franean1_0231; -.
DR   eggNOG; ENOG4105BZ5; Bacteria.
DR   eggNOG; COG0484; LUCA.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; MKIKRKT; -.
DR   OrthoDB; 1738789at2; -.
DR   BioCyc; FSP298653:G1G9X-223-MONOMER; -.
DR   Proteomes; UP000001313; 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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
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; 2.
DR   SUPFAM; SSF57938; SSF57938; 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; A8LDT3.
DR   SWISS-2DPAGE; A8LDT3.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00880482};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01152};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01152};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00880538};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00880439};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01152};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00880462};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00880536}.
FT   DOMAIN       10     75       J. {ECO:0000259|PROSITE:PS50076}.
FT   DOMAIN      160    238       CR-type. {ECO:0000259|PROSITE:PS51188}.
FT   REPEAT      173    180       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      190    197       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      212    219       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      226    233       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   ZN_FING     160    238       CR-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00546}.
FT   METAL       173    173       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       176    176       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       190    190       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       193    193       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       212    212       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       215    215       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       226    226       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       229    229       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
SQ   SEQUENCE   393 AA;  41229 MW;  E97D0FEF15CE77FB CRC64;
     MSVRDMVEKD YYAALGVPKD ASAADIKKAY RKLARELHPD KNPGDVKAEA RFKEVSEAYD
     VLSDENRRRE YDEARALFAS GSYPGAGGRG GGMGGFGTPG GYGPGAGNLN LDDLLNGNGG
     GGLGGIFDNL FQRTPTGRAP RRGTDIAAEV TISFEKSLTG LEATVRLPGA ATCATCAGIG
     ARPGTSPRTC PVCRGLGVIS RSQGGFALSE PCRDCLGKGS LIDHPCPDCH GTGRREREQR
     IRIPAGVSDG QRLRVRGRGS PGERGGAAGD LEVTVHVQSH PVFGREGHNL TINLPVTITE
     AALGASVKVP TIDGTPLTVK VPAGTSSGRR LRARNRGVPR PGGENGDLIV TLEVTVPKPS
     ELSPKARTAL QEFARAHPED PRESLIAQME GRA
//

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