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Q8CWT2 (DNAJ_STRR6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chaperone protein DnaJ
Gene names
Name:dnaJ
Ordered Locus Names:spr0456
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP]
Taxonomic identifier171101 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length372 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.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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
Reference 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Chaperone protein DnaJ HAMAP-Rule MF_01152
PRO_0000070902

Regions

Domain5 – 6965J
Repeat142 – 1498CXXCXGXG motif HAMAP-Rule MF_01152
Repeat159 – 1668CXXCXGXG motif HAMAP-Rule MF_01152
Repeat185 – 1928CXXCXGXG motif HAMAP-Rule MF_01152
Repeat199 – 2068CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger129 – 21183CR-type HAMAP-Rule MF_01152
Compositional bias74 – 11239Gly-rich HAMAP-Rule MF_01152

Sites

Metal binding1421Zinc 1 By similarity
Metal binding1451Zinc 1 By similarity
Metal binding1591Zinc 2 By similarity
Metal binding1621Zinc 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
Q8CWT2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: CAFF00FE14AB07F2

FASTA37240,056
        10         20         30         40         50         60 
MNNTEFYDRL GVSKNASADE IKKAYRKLSK KYHPDINKEP GAEDKYKEVQ EAYETLSDDQ 

        70         80         90        100        110        120 
KRAAYDQYGA AGANGGFGGF NGAGGFGGFE DIFSSFFGGG GSSRNPNAPR QGDDLQYRVN 

       130        140        150        160        170        180 
LTFEEAIFGT EKEVKYHREA GCRTCNGSGA KPGTSPVTCG RCHGAGVINV DTQTPLGMMR 

       190        200        210        220        230        240 
RQVTCDVCHG RGKEIKYPCT TCHGTGHEKQ AHSVHVKIPA GVETGQQIRL AGQGEAGFNG 

       250        260        270        280        290        300 
GPYGDLYVVV SVEASDKFER EGTTIFYNLN LNFVQAALGD TVDIPTVHGD VELVIPEGTQ 

       310        320        330        340        350        360 
TGKKFRLRSK GAPSLRGGAV GDQYVTVNVV TPTGLNDRQK VALKEFAAAG DLKVNPKKKG 

       370 
FFDHIKDAFD GE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE007317 Genomic DNA. Translation: AAK99260.1.
PIRH97928.
RefSeqNP_358050.1. NC_003098.1.

3D structure databases

ProteinModelPortalQ8CWT2.
ModBaseSearch...

Protein-protein interaction databases

STRING171101.spr0456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK99260; AAK99260; spr0456.
GeneID934826.
KEGGspr:spr0456.
PATRIC19700763. VBIStrPne107296_0503.

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226717.
KOK03686.
OMAMRNPNAP.
ProtClustDBPRK14276.

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]
PfamPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. DnaJ_N. 1 hit.
SSF49493. HSP40_DnaJ_pep. 2 hits.
SSF57938. HSP_DnaJ_cys-rich. 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_STRR6
AccessionPrimary (citable) accession number: Q8CWT2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 72 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

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