(data stored in ACNUC1104 zone)

SWISSPROT: D5US62_TSUPD

ID   D5US62_TSUPD            Unreviewed;       400 AA.
AC   D5US62;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN   OrderedLocusNames=Tpau_0488 {ECO:0000313|EMBL:ADG77129.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77129.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77129.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
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; CP001966; ADG77129.1; -; Genomic_DNA.
DR   RefSeq; WP_013125171.1; NC_014158.1.
DR   STRING; 521096.Tpau_0488; -.
DR   EnsemblBacteria; ADG77129; ADG77129; Tpau_0488.
DR   KEGG; tpr:Tpau_0488; -.
DR   eggNOG; ENOG4105BZ5; Bacteria.
DR   eggNOG; COG0484; LUCA.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; MKIKRKT; -.
DR   OrthoDB; 1738789at2; -.
DR   BioCyc; TPAU521096:G1GKO-471-MONOMER; -.
DR   Proteomes; UP000001213; 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   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; D5US62.
DR   SWISS-2DPAGE; D5US62.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00880482};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
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:UP000001213};
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      170    248       CR-type. {ECO:0000259|PROSITE:PS51188}.
FT   REPEAT      183    190       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      200    207       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      222    229       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      236    243       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   ZN_FING     170    248       CR-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00546}.
FT   METAL       183    183       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       186    186       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       200    200       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       203    203       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       222    222       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       225    225       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       236    236       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       239    239       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
SQ   SEQUENCE   400 AA;  41235 MW;  6166F89186EBBA7C CRC64;
     MTQREWVEQD FYRELGVSSD ASQDDIKKAY RKLAAELHPD RNPGDAKAEE RFKRVSEANS
     VLSDPAKRKE YDETRRLFGG GRFGSNGGGF GTGGFGNTGG GTGGFSFSDI FDGATGGGGG
     GFGDIFEGLF NRGGGAPGGA SGSGPQPSRP RRGNDLESEI TLGFRDATLG VTTPITLTSP
     SPCTTCHGSG AKPGTSPRVC QSCNGSGLVS RNQGAFSFSE PCPDCRGTGS VIDDPCTDCS
     GTGVTVRTRT VNVKIPPGVK DGQRIRLAGQ GQAGMRGAPS GDLFVVVHVK ADDVFTRSGD
     DLLVTLPVSF SELALGSTVT VPTLGQPVGV KIPAGTTDGR TLRVRGRGVP KRSGGHGDLL
     VKVQVSVPGS LDEAAQAALR TYAEAEKASG FDPRSGWAGA
//

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