(data stored in SCRATCH zone)

SWISSPROT: C1ASF5_RHOOB

ID   C1ASF5_RHOOB            Unreviewed;       396 AA.
AC   C1ASF5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   05-JUL-2017, entry version 67.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152,
GN   ECO:0000313|EMBL:BAH48404.1};
GN   OrderedLocusNames=ROP_01570 {ECO:0000313|EMBL:BAH48404.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48404.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48404.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48404.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
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: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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP011115; BAH48404.1; -; Genomic_DNA.
DR   RefSeq; WP_012687413.1; NC_012522.1.
DR   ProteinModelPortal; C1ASF5; -.
DR   STRING; 632772.ROP_01570; -.
DR   EnsemblBacteria; BAH48404; BAH48404; ROP_01570.
DR   KEGG; rop:ROP_01570; -.
DR   PATRIC; fig|632772.20.peg.188; -.
DR   eggNOG; ENOG4105BZ5; Bacteria.
DR   eggNOG; COG0484; LUCA.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; ETCEVCT; -.
DR   OrthoDB; POG091H00PT; -.
DR   Proteomes; UP000002212; 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-HAMAP.
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   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   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASF5.
DR   SWISS-2DPAGE; C1ASF5.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00842232};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
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:SAAS00786429};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00786525};
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:SAAS00786407};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00786500}.
FT   DOMAIN       10     75       J. {ECO:0000259|PROSITE:PS50076}.
FT   DOMAIN      165    243       CR-type. {ECO:0000259|PROSITE:PS51188}.
FT   REPEAT      178    185       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      195    202       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      217    224       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      231    238       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   ZN_FING     165    243       CR-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00546}.
FT   METAL       178    178       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       181    181       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       195    195       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       198    198       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       217    217       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       220    220       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       231    231       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       234    234       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
SQ   SEQUENCE   396 AA;  41608 MW;  A7B159876612965C CRC64;
     MTQQEWIERD FYADLGVPST ASAEQIKRAY RTLARRLHPD ANPDDAAAGE RFKAVSEAHA
     VLSDPATRAE YDRTRQLYRS GSFRQAGTRA GAAARSGGGM GGFDLSDLFG SGSAAFTSGD
     AGFGDVFGDL FRRSGTRTTT ASSRPRRGSD VEAQTRLPLR QAVTGVVLPL QVSGPTVCTT
     CHGSGARPGT RPRRCPSCGG AGTLTRNQGG FGFSEPCDDC RGTGMIVDHP CADCQGTGVG
     HRTRTINVRI PPGVTDGQRI RLPAHGEPGL RGAPAGDLYV TVTVDPDPVF GRDGDDLTVT
     VPVGFGELAL GTTISVPTLD GRVSVKIPAG TPSGRTFRLR GRGVHRGGGP AGDLRVTVQV
     AVPTRLDRSA VDALRAYDKA EKATGFDPRA AWPGHR
//

If you have problems or comments...

PBIL Back to PBIL home page