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DNAJ_CAMJE
ID   DNAJ_CAMJE              Reviewed;         373 AA.
AC   O85213; O68797; Q0P8Z6; Q9PN37;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=Cj1260c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F38011;
RX   PubMed=9673247; DOI=10.1128/iai.66.8.3666-3672.1998;
RA   Konkel M.E., Kim B.J., Klena J.D., Young C.R., Ziprin R.;
RT   "Characterization of the thermal stress response of Campylobacter jejuni.";
RL   Infect. Immun. 66:3666-3672(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bras A.M., Wren B.W., Ketley J.M.;
RT   "Characterization of the RacR regulon of Campylobacter jejuni.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC       heat shock by preventing the aggregation of stress-denatured proteins
CC       and by disaggregating proteins, also in an autonomous, DnaK-independent
CC       fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC       with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC       in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC       binding to DnaK triggers the release of the substrate protein, thus
CC       completing the reaction cycle. Several rounds of ATP-dependent
CC       interactions between DnaJ, DnaK and GrpE are required for fully
CC       efficient folding. Also involved, together with DnaK and GrpE, in the
CC       DNA replication of 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 center 2
CC       is essential for interaction with DnaK and for DnaJ activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01152}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC08023.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF052661; AAC32328.1; -; Genomic_DNA.
DR   EMBL; AF053962; AAC08023.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL111168; CAL35375.1; -; Genomic_DNA.
DR   PIR; F81333; F81333.
DR   PIR; T48660; T48660.
DR   RefSeq; WP_002853203.1; NC_002163.1.
DR   RefSeq; YP_002344651.1; NC_002163.1.
DR   AlphaFoldDB; O85213; -.
DR   SMR; O85213; -.
DR   IntAct; O85213; 28.
DR   STRING; 192222.Cj1260c; -.
DR   PaxDb; O85213; -.
DR   PRIDE; O85213; -.
DR   EnsemblBacteria; CAL35375; CAL35375; Cj1260c.
DR   GeneID; 905551; -.
DR   KEGG; cje:Cj1260c; -.
DR   PATRIC; fig|192222.6.peg.1243; -.
DR   eggNOG; COG0484; Bacteria.
DR   HOGENOM; CLU_017633_0_7_7; -.
DR   OMA; GMSAFNG; -.
DR   Proteomes; UP000000799; 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;
KW   Chaperone; Cytoplasm; DNA replication; Metal-binding; Reference proteome;
KW   Repeat; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..373
FT                   /note="Chaperone protein DnaJ"
FT                   /id="PRO_0000070751"
FT   DOMAIN          4..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   REPEAT          148..155
FT                   /note="CXXCXGXG motif"
FT   REPEAT          164..171
FT                   /note="CXXCXGXG motif"
FT   REPEAT          186..193
FT                   /note="CXXCXGXG motif"
FT   REPEAT          200..207
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         135..212
FT                   /note="CR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   CONFLICT        57
FT                   /note="S -> T (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71..72
FT                   /note="DA -> M (in Ref. 1; AAC32328)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="G -> A (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="S -> T (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="M -> I (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="S -> F (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="E -> D (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="T -> A (in Ref. 2; AAC08023)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   373 AA;  41523 MW;  653F46CBF489D2CD CRC64;
     MEISYYEILE ITQNADKETI KKAYRKMALK YHPDRNQGDK EAEDKFKLVN EAYEVLSNDE
     KRAIYDRYGK DALKGGGFGS SSSGFGGFED LGDIFSSFFG EGFGSSRRRK SSNDEKIPSD
     FIVNLKLSFK EAVFGCKKNI DFTYKCSCKT CNGTGAKDGK LQTCPKCQGR GQVGVSQGFI
     TFAQTCPDCQ GIGEKASEKC SDCKGLGYNE SKDSVELNIP EGVDTGMKLR VNAKGNILKN
     GTRGDMYVKI IAAEDDTFIR DDDDIYIEFP VFFTQAILGE SIKVPTIRGE ATLNLPKGAK
     DGQRFVLEKE GVKDVHSSRM GNQIVQISIK FPTSLNDEQK ELLEKLSESF GIKDGMHQEQ
     KGLFEKITNW FKS
 
 
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