DNAJ_AGRFC
ID DNAJ_AGRFC Reviewed; 377 AA.
AC P50018;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=Atu0121;
GN ORFNames=AGR_C_192;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RX PubMed=7592349; DOI=10.1128/jb.177.20.5952-5958.1995;
RA Segal G., Ron E.Z.;
RT "The dnaKJ operon of Agrobacterium tumefaciens: transcriptional analysis
RT and evidence for a new heat shock promoter.";
RL J. Bacteriol. 177:5952-5958(1995).
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 -!- INDUCTION: By heat shock.
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}.
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DR EMBL; AE007869; AAK85941.1; -; Genomic_DNA.
DR EMBL; X87113; CAA60593.1; -; Genomic_DNA.
DR PIR; AD2591; AD2591.
DR PIR; D97373; D97373.
DR PIR; I39586; I39586.
DR RefSeq; NP_353156.1; NC_003062.2.
DR RefSeq; WP_006309945.1; NC_003062.2.
DR AlphaFoldDB; P50018; -.
DR SMR; P50018; -.
DR STRING; 176299.Atu0121; -.
DR PRIDE; P50018; -.
DR DNASU; 1132159; -.
DR EnsemblBacteria; AAK85941; AAK85941; Atu0121.
DR GeneID; 66223132; -.
DR KEGG; atu:Atu0121; -.
DR PATRIC; fig|176299.10.peg.113; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_7_5; -.
DR OMA; DLHCTVT; -.
DR PhylomeDB; P50018; -.
DR BioCyc; AGRO:ATU0121-MON; -.
DR Proteomes; UP000000813; Chromosome circular.
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 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Reference proteome;
KW Repeat; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..377
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000070708"
FT DOMAIN 5..70
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 151..158
FT /note="CXXCXGXG motif"
FT REPEAT 168..175
FT /note="CXXCXGXG motif"
FT REPEAT 190..197
FT /note="CXXCXGXG motif"
FT REPEAT 204..211
FT /note="CXXCXGXG motif"
FT ZN_FING 138..216
FT /note="CR-type"
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 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT CONFLICT 4
FT /note="A -> R (in Ref. 3; CAA60593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 40894 MW; 0E68A1D30754D18A CRC64;
MAKADFYETL GVSKTADEKE LKSAFRKLAM KFHPDKNPDD ADSERKFKEI NEAYETLKDP
QKRAAYDRFG HAAFENGGMG GGGMGGGGFA NGGFSDIFED IFGEMMGGGR ARRSSGGRER
GADLRYNMEI TLEEAFAGKT AQIRVPTSIT CDVCSGSGAK PGTQPKTCAT CQGSGRVRAA
QGFFSVERTC PTCHGRGQTI SDPCGKCHGQ GRVTEERSLS VNIPSGIEDG TRIRLQGEGE
AGMRGGPAGD LYIFLSVRPH EFFQRDGADL YCTVPISMTT AALGGTFDVT TLDGTKSRVT
VPEGTQPGKQ FRLKGKGMPV LRSAQTGDLY IQIQIETPQK LSKRQRELLQ EFEQLSSKEN
NPESTGFFAR MKEFFDG
