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Q8K9Y9 (DNAJ_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone protein DnaJ
Gene names
Name:dnaJ
Ordered Locus Names:BUsg_145
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins By similarity. HAMAP-Rule MF_01152

Cofactor

Binds 2 zinc ions per monomer By similarity. HAMAP-Rule MF_01152

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01152

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01152.

Domain

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 By similarity. HAMAP-Rule MF_01152

Sequence similarities

Belongs to the DnaJ family.

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Ontologies

Keywords
   Biological processDNA replication
Stress response
   Cellular componentCytoplasm
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: InterPro

response to heat

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Chaperone protein DnaJ HAMAP-Rule MF_01152
PRO_0000070746

Regions

Domain5 – 7066J
Repeat146 – 1538CXXCXGXG motif HAMAP-Rule MF_01152
Repeat163 – 1708CXXCXGXG motif HAMAP-Rule MF_01152
Repeat185 – 1928CXXCXGXG motif HAMAP-Rule MF_01152
Repeat199 – 2068CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger133 – 21179CR-type HAMAP-Rule MF_01152
Compositional bias77 – 11640Gly-rich HAMAP-Rule MF_01152

Sites

Metal binding1461Zinc 1 By similarity
Metal binding1491Zinc 1 By similarity
Metal binding1631Zinc 2 By similarity
Metal binding1661Zinc 2 By similarity
Metal binding1851Zinc 2 By similarity
Metal binding1881Zinc 2 By similarity
Metal binding1991Zinc 1 By similarity
Metal binding2021Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9Y9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: BB73F48DAF7A2D34

FASTA37842,469
        10         20         30         40         50         60 
MAKKDYYQIL GIPKSAEERE IKKAYKRLAM KYHPDRNQGD KNAENKFKEI KEAYEILINE 

        70         80         90        100        110        120 
EKRTAYDQYG HAAFENGYNQ NNTYSTFTSS TDFGDIFGDV FGDIFGGSRN QRVKKGADLC 

       130        140        150        160        170        180 
YNMEISLEEA VKGTTKEIRI PTFQKCKTCY GMGTSTGTKP NGCSTCHGKG QIHIRKGFFT 

       190        200        210        220        230        240 
VQQSCPTCNG IGTVIKNPCR MCRGQGRIKT NKTLSVKIPP GIDTNDKIRL SKEGEAGTNG 

       250        260        270        280        290        300 
AQPGDLYVQM KVNKHPIFER EENNLYCEVP INFTMAALGG EIEVPTLDGR VNLKIPSETQ 

       310        320        330        340        350        360 
SGKLFRIRGK GVKSVQSRSR GDLLCRVVVE TPVNLNEKQK YLLSELGNSF NGFRGDKNSP 

       370 
RSKRFFDGVK RFFDDLTK 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67713.1.
RefSeqNP_660502.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Y9.
SMRQ8K9Y9. Positions 2-77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67713; AAM67713; BUsg_145.
GeneID1005962.
KEGGbas:BUsg145.
PATRIC21247071. VBIBucAph100086_0149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0484.
KOK03686.
OMAVDDGQQL.
OrthoDBEOG6BPDKP.
ProtClustDBPRK10767.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-155-MONOMER.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPMF_01152. DnaJ.
InterProIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
TIGRFAMsTIGR02349. DnaJ_bact. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDNAJ_BUCAP
AccessionPrimary (citable) accession number: Q8K9Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names