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P08622

- DNAJ_ECOLI

UniProt

P08622 - DNAJ_ECOLI

Protein

Chaperone protein DnaJ

Gene

dnaJ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.4 Publications

    Cofactori

    Binds 2 zinc ions per monomer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi144 – 1441Zinc 1
    Metal bindingi147 – 1471Zinc 1
    Metal bindingi161 – 1611Zinc 2
    Metal bindingi164 – 1641Zinc 2
    Metal bindingi183 – 1831Zinc 2
    Metal bindingi186 – 1861Zinc 2
    Metal bindingi197 – 1971Zinc 1
    Metal bindingi200 – 2001Zinc 1

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri131 – 20979CR-typeAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. protein binding Source: IntAct
    3. protein disulfide isomerase activity Source: EcoliWiki
    4. unfolded protein binding Source: EcoliWiki
    5. zinc ion binding Source: EcoliWiki

    GO - Biological processi

    1. DNA replication Source: EcoliWiki
    2. protein folding Source: EcoliWiki
    3. protein refolding Source: EcoliWiki
    4. protein unfolding Source: EcoCyc
    5. response to heat Source: EcoliWiki

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    DNA replication, Stress response

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10240-MONOMER.
    ECOL316407:JW0014-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chaperone protein DnaJ
    Alternative name(s):
    HSP40
    Heat shock protein J
    Gene namesi
    Name:dnaJ
    Synonyms:groP
    Ordered Locus Names:b0015, JW0014
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10240. dnaJ.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. membrane Source: EcoliWiki

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Single dnaJ and double dnaK-dnaJ disruption are non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at 43 degrees) and strain background.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 202RE → AA: No effect. 1 Publication
    Mutagenesisi25 – 251Y → A: Loss of activity.
    Mutagenesisi26 – 261K → A: Loss of activity.
    Mutagenesisi27 – 271R → A: No effect.
    Mutagenesisi28 – 281L → A: No effect.
    Mutagenesisi29 – 291A → G: No effect.
    Mutagenesisi30 – 312MK → AA: No effect.
    Mutagenesisi32 – 321Y → A: No effect.
    Mutagenesisi33 – 331H → Q: Loss of ability to stimulate DnaK ATPase activity. 1 Publication
    Mutagenesisi34 – 341P → F: Loss of function.
    Mutagenesisi35 – 351D → N: Loss of ability to bind DnaK. 1 Publication
    Mutagenesisi36 – 361R → A: Decrease in chaperone function.
    Mutagenesisi37 – 371N → A: Decrease in chaperone function.
    Mutagenesisi38 – 381Q → A: No effect.
    Mutagenesisi41 – 422KE → AA: No effect. 1 Publication
    Mutagenesisi44 – 441E → A: No effect. 1 Publication
    Mutagenesisi46 – 461K → A: No effect.
    Mutagenesisi47 – 471F → A: Loss of function.
    Mutagenesisi48 – 492KE → AA: No effect.
    Mutagenesisi51 – 522KE → AA: No effect. 1 Publication
    Mutagenesisi54 – 541Y → A: No effect. 1 Publication
    Mutagenesisi55 – 551E → A: No effect. 1 Publication
    Mutagenesisi58 – 592TD → AA: No effect.
    Mutagenesisi60 – 612SQ → AA: No effect.
    Mutagenesisi62 – 632KR → AA: No effect.
    Mutagenesisi67 – 682DQ → AA: No effect. 1 Publication
    Mutagenesisi144 – 1441C → S: Loss of DnaK-independent chaperone activity; when associated with S-147; S-197 and S-200. 1 Publication
    Mutagenesisi147 – 1471C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-197 and S-200. 1 Publication
    Mutagenesisi161 – 1611C → H: No effect on chaperone function; when associated with H-183. 2 Publications
    Mutagenesisi161 – 1611C → S: Loss of function; when associated with S-164; S-183 and S-186. 2 Publications
    Mutagenesisi164 – 1641C → H: No effect on chaperone function; when associated with H-183. 2 Publications
    Mutagenesisi164 – 1641C → S: Loss of function; when associated with S-161; S-183 and S-186. 2 Publications
    Mutagenesisi183 – 1831C → H: No effect on chaperone function. Same effect; when associated with H-161 or H-164. 2 Publications
    Mutagenesisi183 – 1831C → S: Loss of function; when associated with S-161; S-164 and S-186. 2 Publications
    Mutagenesisi186 – 1861C → H: No effect on chaperone function. 2 Publications
    Mutagenesisi186 – 1861C → S: Loss of function; when associated with S-161; S-164 and S-184. 2 Publications
    Mutagenesisi197 – 1971C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-200. 1 Publication
    Mutagenesisi200 – 2001C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-197. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 376375Chaperone protein DnaJPRO_0000070777Add
    BLAST

    Proteomic databases

    PaxDbiP08622.
    PRIDEiP08622.

    Expressioni

    Inductioni

    By heat shock under the control of the HtpR regulatory protein.

    Gene expression databases

    GenevestigatoriP08622.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaKP0A6Y85EBI-545285,EBI-542092
    malTP069933EBI-545285,EBI-542934

    Protein-protein interaction databases

    BioGridi849156. 1 interaction.
    DIPiDIP-9460N.
    IntActiP08622. 95 interactions.
    MINTiMINT-1220303.
    STRINGi511145.b0015.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni7 – 104
    Beta strandi13 – 153
    Helixi18 – 2912
    Turni30 – 323
    Turni34 – 363
    Turni38 – 403
    Helixi43 – 508
    Turni51 – 555
    Helixi61 – 655
    Turni66 – 683
    Turni70 – 723
    Turni132 – 1343
    Beta strandi141 – 1433
    Helixi145 – 1473
    Turni148 – 1503
    Beta strandi154 – 1563
    Turni162 – 1665
    Beta strandi167 – 1748
    Beta strandi177 – 1826
    Turni184 – 1885
    Beta strandi189 – 1924
    Beta strandi194 – 1963
    Helixi198 – 2003
    Beta strandi203 – 2075

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQ0NMR-A2-104[»]
    1BQZNMR-A2-78[»]
    1EXKNMR-A131-209[»]
    1XBLNMR-A2-108[»]
    ProteinModelPortaliP08622.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08622.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7270JAdd
    BLAST
    Repeati144 – 1518CXXCXGXG motif
    Repeati161 – 1688CXXCXGXG motif
    Repeati183 – 1908CXXCXGXG motif
    Repeati197 – 2048CXXCXGXG motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi77 – 11438Gly-richAdd
    BLAST

    Domaini

    The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.

    Sequence similaritiesi

    Belongs to the DnaJ family.Curated
    Contains 1 CR-type zinc finger.Curated
    Contains 1 J domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri131 – 20979CR-typeAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0484.
    HOGENOMiHOG000226717.
    KOiK03686.
    OMAiCHGNGQV.
    OrthoDBiEOG6BPDKP.
    PhylomeDBiP08622.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    2.10.230.10. 1 hit.
    HAMAPiMF_01152. DnaJ.
    InterProiIPR012724. DnaJ.
    IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    IPR001305. HSP_DnaJ_Cys-rich_dom.
    [Graphical view]
    PfamiPF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    PF00684. DnaJ_CXXCXGXG. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 3 hits.
    SSF57938. SSF57938. 1 hit.
    TIGRFAMsiTIGR02349. DnaJ_bact. 1 hit.
    PROSITEiPS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51188. ZF_CR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08622-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI    50
    KEAYEVLTDS QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD 100
    IFGGGRGRQR AARGADLRYN MELTLEEAVR GVTKEIRIPT LEECDVCHGS 150
    GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ QTCPHCQGRG TLIKDPCNKC 200
    HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP AGDLYVQVQV 250
    KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG 300
    KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG 350
    PTGEHNSPRS KSFFDGVKKF FDDLTR 376
    Length:376
    Mass (Da):41,100
    Last modified:January 23, 2007 - v3
    Checksum:i05FA762EF9844532
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12544 Genomic DNA. Translation: AAA00009.1.
    M12565 Genomic DNA. Translation: AAA23693.1.
    U00096 Genomic DNA. Translation: AAC73126.1.
    AP009048 Genomic DNA. Translation: BAB96590.1.
    PIRiA92572. HHECDJ.
    RefSeqiNP_414556.1. NC_000913.3.
    YP_488321.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73126; AAC73126; b0015.
    BAB96590; BAB96590; BAB96590.
    GeneIDi12930731.
    944753.
    KEGGiecj:Y75_p0015.
    eco:b0015.
    PATRICi32115123. VBIEscCol129921_0013.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12544 Genomic DNA. Translation: AAA00009.1 .
    M12565 Genomic DNA. Translation: AAA23693.1 .
    U00096 Genomic DNA. Translation: AAC73126.1 .
    AP009048 Genomic DNA. Translation: BAB96590.1 .
    PIRi A92572. HHECDJ.
    RefSeqi NP_414556.1. NC_000913.3.
    YP_488321.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BQ0 NMR - A 2-104 [» ]
    1BQZ NMR - A 2-78 [» ]
    1EXK NMR - A 131-209 [» ]
    1XBL NMR - A 2-108 [» ]
    ProteinModelPortali P08622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 849156. 1 interaction.
    DIPi DIP-9460N.
    IntActi P08622. 95 interactions.
    MINTi MINT-1220303.
    STRINGi 511145.b0015.

    Proteomic databases

    PaxDbi P08622.
    PRIDEi P08622.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73126 ; AAC73126 ; b0015 .
    BAB96590 ; BAB96590 ; BAB96590 .
    GeneIDi 12930731.
    944753.
    KEGGi ecj:Y75_p0015.
    eco:b0015.
    PATRICi 32115123. VBIEscCol129921_0013.

    Organism-specific databases

    EchoBASEi EB0236.
    EcoGenei EG10240. dnaJ.

    Phylogenomic databases

    eggNOGi COG0484.
    HOGENOMi HOG000226717.
    KOi K03686.
    OMAi CHGNGQV.
    OrthoDBi EOG6BPDKP.
    PhylomeDBi P08622.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10240-MONOMER.
    ECOL316407:JW0014-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P08622.
    PROi P08622.

    Gene expression databases

    Genevestigatori P08622.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    2.10.230.10. 1 hit.
    HAMAPi MF_01152. DnaJ.
    InterProi IPR012724. DnaJ.
    IPR002939. DnaJ_C.
    IPR001623. DnaJ_domain.
    IPR018253. DnaJ_domain_CS.
    IPR008971. HSP40/DnaJ_pept-bd.
    IPR001305. HSP_DnaJ_Cys-rich_dom.
    [Graphical view ]
    Pfami PF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    PF00684. DnaJ_CXXCXGXG. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 3 hits.
    SSF57938. SSF57938. 1 hit.
    TIGRFAMsi TIGR02349. DnaJ_bact. 1 hit.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51188. ZF_CR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product."
      Ohki M., Tamura F., Nishimura S., Uchida H.
      J. Biol. Chem. 261:1778-1781(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6.
    2. "The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein."
      Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M., Georgopoulos C.
      J. Biol. Chem. 261:1782-1785(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK."
      Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M.
      Proc. Natl. Acad. Sci. U.S.A. 88:2874-2878(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation."
      Zietkiewicz S., Krzewska J., Liberek K.
      J. Biol. Chem. 279:44376-44383(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Immediate response of the DnaK molecular chaperone system to heat shock."
      Siegenthaler R.K., Grimshaw J.P., Christen P.
      FEBS Lett. 562:105-110(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN HEAT-SHOCK RESPONSE.
    10. "In vivo analysis of the overlapping functions of DnaK and trigger factor."
      Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U., Georgopoulos C.
      EMBO Rep. 5:195-200(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    11. "Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB."
      Watanabe Y.H., Yoshida M.
      J. Biol. Chem. 279:15723-15727(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAK.
    12. "The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation."
      Zzaman S., Reddy J.M., Bastia D.
      J. Biol. Chem. 279:50886-50894(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN PLASMID DNA REPLICATION.
    13. "The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication."
      Wall D., Zylicz M., Georgopoulos C.
      J. Biol. Chem. 269:5446-5451(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-33.
    14. "Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ."
      Suh W.-C., Burkholder W.F., Lu C.Z., Zhao X., Gottesman M.E., Gross C.A.
      Proc. Natl. Acad. Sci. U.S.A. 95:15223-15228(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-35.
    15. "Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain."
      Genevaux P., Schwager F., Georgopoulos C., Kelley W.L.
      Genetics 162:1045-1053(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-19; GLU-20; 25-TYR--GLN-38; LYS-41; GLU-42; GLU-44; 46-LYS--GLU-49; LYS-51; GLU-52; TYR-54; GLU-55; 58-THR--ARG-63; ASP-67 AND GLN-68.
    16. "The roles of the two zinc binding sites in DnaJ."
      Linke K., Wolfram T., Bussemer J., Jakob U.
      J. Biol. Chem. 278:44457-44466(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-144; CYS-147; CYS-161; CYS-164; CYS-183; CYS-186; CYS-197 AND CYS-200.
    17. "Contributions of cysteine residues in Zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ."
      Shi Y.-Y., Tang W., Hao S.-F., Wang C.-C.
      Biochemistry 44:1683-1689(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-161; CYS-164; CYS-183 AND CYS-186.
    18. "NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone."
      Pellechia M., Szyperski T., Wall D., Georgopoulos C., Wuethrich K.
      J. Mol. Biol. 260:236-250(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-108.
    19. "The influence of C-terminal extension on the structure of the 'J-domain' in E. coli DnaJ."
      Huang K., Flanagan J.M., Prestegard J.H.
      Protein Sci. 8:203-214(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-105.
    20. "Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ."
      Martinez-Yamout M., Legge G.B., Zhang O., Wright P.E., Dyson H.J.
      J. Mol. Biol. 300:805-818(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 131-209.

    Entry informationi

    Entry nameiDNAJ_ECOLI
    AccessioniPrimary (citable) accession number: P08622
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3