(data stored in SCRATCH zone)

SWISSPROT: C7QH99_CATAD

ID   C7QH99_CATAD            Unreviewed;       374 AA.
AC   C7QH99;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-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   OrderedLocusNames=Caci_0083 {ECO:0000313|EMBL:ACU69038.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69038.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69038.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU69038.1; -; Genomic_DNA.
DR   RefSeq; WP_012784333.1; NC_013131.1.
DR   ProteinModelPortal; C7QH99; -.
DR   STRING; 479433.Caci_0083; -.
DR   PRIDE; C7QH99; -.
DR   EnsemblBacteria; ACU69038; ACU69038; Caci_0083.
DR   KEGG; cai:Caci_0083; -.
DR   eggNOG; ENOG4105BZ5; Bacteria.
DR   eggNOG; COG0484; LUCA.
DR   eggNOG; COG2214; LUCA.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; KEGMMDH; -.
DR   OrthoDB; POG091H00PT; -.
DR   Proteomes; UP000000851; 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   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; C7QH99.
DR   SWISS-2DPAGE; C7QH99.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00842232};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
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   Reference proteome {ECO:0000313|Proteomes:UP000000851};
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        6     71       J. {ECO:0000259|PROSITE:PS50076}.
FT   DOMAIN      141    219       CR-type. {ECO:0000259|PROSITE:PS51188}.
FT   REPEAT      154    161       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      171    178       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      193    200       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      207    214       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   ZN_FING     141    219       CR-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00546}.
FT   METAL       154    154       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       157    157       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       171    171       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       174    174       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       193    193       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       196    196       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       207    207       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       210    210       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
SQ   SEQUENCE   374 AA;  39328 MW;  31553A6DF9201FAF CRC64;
     MAVNKDYYKI LGVPKDAPAA DIKKAYRKLA RQYHPDANKG DAASEEKFKE ISEAYDVLSD
     DKRRKEYDDS RSVFGNGGFR APGGGAPGGF NFDLGDLLGG LFNRTGGPTT GTSTTGRTTQ
     ARRGSDVESE VTLKFSDSID GATVSLRLTS DTPCSACSGT GAKAGTTPRV CPTCSGTGQV
     SRNQGGFAFS EPCRDCKGRG LLVDDPCPVC HGSGRAASSR TIQARIPAGV RDGQRIRLKG
     KGASGERGGP AGDLYVVVHV SPHPVFGRED DNLTVTVPVT FPEAVLGADI QVPTLGGMPV
     TVKLPANSQN GRVLRVRGRG VARKDGTKGD LLVRFEIAVP AEIGDDARAA LQKFQEATGN
     HHPRAELLDS AKGE
//

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