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
