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Database: UniProt
Entry: P35514
LinkDB: P35514
Original site: P35514 
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   26-NOV-2014, entry version 109.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=LL2224;
GN   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.
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
CC       center 2 is essential for interaction with DnaK and for DnaJ
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01152}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01152}.
CC   -!- SIMILARITY: Contains 1 CR-type zinc finger. {ECO:0000255|HAMAP-
CC       Rule:MF_01152}.
CC   -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01152}.
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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; TCHGNGA; -.
DR   OrthoDB; EOG6BPDKP; -.
DR   BioCyc; LLAC272623:GHSH-2366-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   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; PF01556; CTDII; 1.
DR   Pfam; PF00226; DnaJ; 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;
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. {ECO:0000255|HAMAP-Rule:MF_01152}.
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. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   COMPBIAS     74    124       Gly-rich.
FT   METAL       154    154       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       157    157       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       171    171       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       174    174       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       197    197       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       200    200       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       211    211       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       214    214       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   CONFLICT     94     94       G -> S (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    164    164       A -> R (in Ref. 1). {ECO:0000305}.
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
//
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