ID DNAJ_LACLA Reviewed; 379 AA.
AC P35514;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 01-MAY-2013, entry version 100.
DE RecName: Full=Chaperone protein DnaJ;
GN Name=dnaJ; OrderedLocusNames=LL2224; ORFNames=L0272;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIZO R5;
RX PubMed=8449872;
RA van Asseldonk M., Simons A., Visser H., de Vos W.M., Simons G.;
RT "Cloning, nucleotide sequence, and regulatory analysis of the
RT Lactococcus lactis dnaJ gene.";
RL J. Bacteriol. 175:1637-1644(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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 (By
CC similarity).
CC -!- COFACTOR: Binds 2 zinc ions per monomer (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the DnaJ family.
CC -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC -!- SIMILARITY: Contains 1 J domain.
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DR EMBL; M99413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE005176; AAK06322.1; -; Genomic_DNA.
DR PIR; A47079; A47079.
DR PIR; H86902; H86902.
DR RefSeq; NP_268381.1; NC_002662.1.
DR ProteinModelPortal; P35514; -.
DR STRING; 272623.L0272; -.
DR EnsemblBacteria; AAK06322; AAK06322; L0272.
DR GeneID; 1115902; -.
DR KEGG; lla:L0272; -.
DR PATRIC; 22297012; VBILacLac136773_2389.
DR eggNOG; COG0484; -.
DR HOGENOM; HOG000226717; -.
DR KO; K03686; -.
DR OMA; ERINKRD; -.
DR ProtClustDB; PRK14276; -.
DR BioCyc; LLAC272623:GHSH-2381-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA: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 Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.10.230.10; -; 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; DnaJ_N; 1.
DR SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 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; Complete proteome; Cytoplasm; DNA replication;
KW Metal-binding; Reference proteome; Repeat; Stress response; Zinc;
KW Zinc-finger.
FT CHAIN 1 379 Chaperone protein DnaJ.
FT /FTId=PRO_0000070802.
FT DOMAIN 5 69 J.
FT REPEAT 154 161 CXXCXGXG motif.
FT REPEAT 171 178 CXXCXGXG motif.
FT REPEAT 197 204 CXXCXGXG motif.
FT REPEAT 211 218 CXXCXGXG motif.
FT ZN_FING 141 223 CR-type.
FT COMPBIAS 74 124 Gly-rich.
FT METAL 154 154 Zinc 1 (By similarity).
FT METAL 157 157 Zinc 1 (By similarity).
FT METAL 171 171 Zinc 2 (By similarity).
FT METAL 174 174 Zinc 2 (By similarity).
FT METAL 197 197 Zinc 2 (By similarity).
FT METAL 200 200 Zinc 2 (By similarity).
FT METAL 211 211 Zinc 1 (By similarity).
FT METAL 214 214 Zinc 1 (By similarity).
FT CONFLICT 94 94 G -> S (in Ref. 1).
FT CONFLICT 164 164 A -> R (in Ref. 1).
SQ SEQUENCE 379 AA; 40671 MW; 399CA4EDCB7067B6 CRC64;
MNNTEYYERL GVDKNASQDE IKKAYRKMSK KYHPDLNKEE GAEEKYKEVQ EAYETLSDEQ
KRAAYDQYGE AGANGGFGGG GFGGASGFSG FGGGSGGFGG FEDIFSSFFG GGGAQVNPNA
PRQGDDLQYR INLKFEEAIF GVEKQVKYNR EELCHTCGGS GAKAGTHPET CHKCGGRGQI
NVVRDTPLGR MQTQVTCDVC NGTGKEIKEK CETCHGSGHE KVAHTVKVTV PAGVETGQKM
RLQGQGDAGV NGGPYGDLYV VFQVEASDKF ERDGAEIYYK MPMDFVQAAL GDEIEVPTVH
GNVKLKIPAG TQTGANFRLK GKGAPKLRGS GNGDQYVIIN IVTPKNLNQA QKEALQAFAK
ASGVEVSGSG KKGFFDKFK
//
