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Database: UniProt
Entry: Q6KHF9
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ID   DNAJ_MYCMO              Reviewed;         373 AA.
AC   Q6KHF9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   26-NOV-2014, entry version 75.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   OrderedLocusNames=MMOB4850;
OS   Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=267748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX   PubMed=15289470; DOI=10.1101/gr.2674004;
RA   Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S.,
RA   Butler J., Calvo S., Elkins T., FitzGerald M.G., Hafez N.,
RA   Kodira C.D., Major J., Wang S., Wilkinson J., Nicol R., Nusbaum C.,
RA   Birren B., Berg H.C., Church G.M.;
RT   "The complete genome and proteome of Mycoplasma mobile.";
RL   Genome Res. 14:1447-1461(2004).
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; AE017308; AAT27971.1; -; Genomic_DNA.
DR   RefSeq; WP_011265005.1; NC_006908.1.
DR   RefSeq; YP_016182.1; NC_006908.1.
DR   ProteinModelPortal; Q6KHF9; -.
DR   SMR; Q6KHF9; 2-73.
DR   STRING; 267748.MMOB4850; -.
DR   EnsemblBacteria; AAT27971; AAT27971; MMOB4850.
DR   GeneID; 2807483; -.
DR   KEGG; mmo:MMOB4850; -.
DR   PATRIC; 20016349; VBIMycMob32482_0511.
DR   eggNOG; COG0484; -.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; CHECHGT; -.
DR   OrthoDB; EOG6BPDKP; -.
DR   BioCyc; MMOB267748:GH6Y-514-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    373       Chaperone protein DnaJ.
FT                                /FTId=PRO_0000070828.
FT   DOMAIN        4     68       J. {ECO:0000255|HAMAP-Rule:MF_01152}.
FT   REPEAT      155    162       CXXCXGXG motif.
FT   REPEAT      172    179       CXXCXGXG motif.
FT   REPEAT      198    205       CXXCXGXG motif.
FT   REPEAT      212    219       CXXCXGXG motif.
FT   ZN_FING     142    224       CR-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   COMPBIAS     74    125       Gly-rich.
FT   METAL       155    155       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       158    158       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       172    172       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       175    175       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       198    198       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       201    201       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       212    212       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
FT   METAL       215    215       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01152}.
SQ   SEQUENCE   373 AA;  41564 MW;  4F7D4DBAF78A4DD3 CRC64;
     MKKDYYEILG LTKSASKDEI KKAYRTLAKT YHPDVNKETN AEEKFKEITE AYEILNDDVK
     REQYNQFGHA AFDPNAGGFG GQNPFTNAEG FSGFSDFSGF GSIFTDFFGG FGNSQRANPN
     RAQRGEDRHA VIKISFIDSV LGKEIVEPLE KFETCNTCNG SGAKSQSDII TCTQCSGMGE
     QIKITKTFLG QMQQNVICSK CNGIGKEIVE KCLICKGKTH TKTTKNITIK IPAGIQNGQT
     LRVENYGNAG LNGGSNGNLI LSIKVSPHKH FVRKNNDIIL RLPVSIKSVI GSEKVEVPTP
     YGFEIIKIDP NIKTGDELII KNKGIITKYE SGKMIVIFEI FIPKLTSFEK KEISTILEKN
     ADKFYEKWIK EFE
//
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