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P08622

- DNAJ_ECOLI

UniProt

P08622 - DNAJ_ECOLI

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Protein
Chaperone protein DnaJ
Gene
dnaJ, groP, b0015, JW0014
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-typeUniRule annotation
Add
BLAST

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: InterPro
  2. protein bindingInferred from physical interactioni PubMed 10521435PubMed 15690043PubMed 18394994PubMed 24561554 Source: IntAct
  3. protein disulfide isomerase activityInferred from direct assayi PubMed 7559385 Source: EcoliWiki
  4. unfolded protein bindingInferred from direct assayi PubMed 7559385 Source: EcoliWiki
  5. zinc ion bindingInferred from direct assayi PubMed 11985624PubMed 8662861 Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. DNA replicationInferred from mutant phenotypei PubMed 2144273 Source: EcoliWiki
  2. protein foldingInferred from direct assayi PubMed 7559385 Source: EcoliWiki
  3. protein refoldingInferred from direct assayi PubMed 7559385 Source: EcoliWiki
  4. protein unfoldingInferred from direct assayi PubMed 20953191 Source: EcoCyc
  5. response to heatInferred from expression patterni PubMed 8349564 Source: EcoliWiki
  1. protein disulfide isomerase activityInferred from direct assayi PubMed 7559385 Source: EcoliWiki
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasmInferred from direct assayi PubMed 6220698 Source: EcoliWiki
  2. membraneInferred from direct assayi PubMed 3889001PubMed 6220698 Source: EcoliWiki
Complete GO annotation...

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 DnaJUniRule annotation
PRO_0000070777Add
BLAST

Proteomic databases

PaxDbiP08622.
PRIDEiP08622.

Expressioni

Inductioni

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

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

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.

Miscellaneous databases

EvolutionaryTraceiP08622.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7270J
Add
BLAST
Repeati144 – 1518CXXCXGXG motifUniRule annotation
Repeati161 – 1688CXXCXGXG motifUniRule annotation
Repeati183 – 1908CXXCXGXG motifUniRule annotation
Repeati197 – 2048CXXCXGXG motifUniRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 11438Gly-richUniRule annotation
Add
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.UniRule annotation

Sequence similaritiesi

Belongs to the DnaJ family.
Contains 1 J domain.

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]FASTA

« 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.
PIRiHHECDJ. A92572.
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 HHECDJ. A92572.
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...

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

« Hide 'large scale' publicationsDownload
  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. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    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 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: July 9, 2014
This is version 162 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

External Data

Dasty 3

Similar proteinsi