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A1RGN2 (DNAJ_SHESW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. 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:Sputw3181_0977
OrganismShewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP]
Taxonomic identifier351745 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length376 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
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 – 376376Chaperone protein DnaJ HAMAP-Rule MF_01152
PRO_1000085300

Regions

Domain5 – 7066J
Repeat145 – 1528CXXCXGXG motif HAMAP-Rule MF_01152
Repeat162 – 1698CXXCXGXG motif HAMAP-Rule MF_01152
Repeat184 – 1918CXXCXGXG motif HAMAP-Rule MF_01152
Repeat198 – 2058CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger132 – 21079CR-type HAMAP-Rule MF_01152
Compositional bias77 – 11539Gly-rich HAMAP-Rule MF_01152

Sites

Metal binding1451Zinc 1 By similarity
Metal binding1481Zinc 1 By similarity
Metal binding1621Zinc 2 By similarity
Metal binding1651Zinc 2 By similarity
Metal binding1841Zinc 2 By similarity
Metal binding1871Zinc 2 By similarity
Metal binding1981Zinc 1 By similarity
Metal binding2011Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1RGN2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: CC2FD660033D35DD

FASTA37640,737
        10         20         30         40         50         60 
MSKRDYYEVL GVGRDASERE IKKAYKRLAM KFHPDRNPGD KAAEASFKEA KEAYEILTDT 

        70         80         90        100        110        120 
DKKAAYDQFG HAGVDPNRGG GYGGGQGDFG DIFGDVFGDI FGGGRRGGQR QAARGSDLRY 

       130        140        150        160        170        180 
NLELSLEEAV KGLTKELRIP TLATCDLCDG SGAKKGTSAS TCTTCHGQGQ VQMRQGFFTV 

       190        200        210        220        230        240 
QQPCPTCHGR GKIIKDPCSK CHGDGRVEKS KTLSVKIPAG VDTGDRIRLA GEGEAGEFGA 

       250        260        270        280        290        300 
PPGDLYVQVS VREHAIFVRD GNNLYCEVPI SFSKAALGGE IEVPTLDGKV SLKIPAETQT 

       310        320        330        340        350        360 
GRMFRLRGKG VKSVRSHAVG DLLCKVVMET PVNLNDRQKE LLREFEATLT GESKKHSPKA 

       370 
EGFFDGVKKF FQDLNS

« Hide

References

[1]"Complete sequence of Shewanella sp. W3-18-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W3-18-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000503 Genomic DNA. Translation: ABM23827.1.
RefSeqYP_962381.1. NC_008750.1.

3D structure databases

ProteinModelPortalA1RGN2.
SMRA1RGN2. Positions 2-75, 132-210.
ModBaseSearch...

Protein-protein interaction databases

STRING351745.Sputw3181_0977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM23827; ABM23827; Sputw3181_0977.
GeneID4659522.
KEGGshw:Sputw3181_0977.
PATRIC23595423. VBISheSp103602_1015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226717.
KOK03686.
OMANKCHGEG.
ProtClustDBPRK10767.

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_SHESW
AccessionPrimary (citable) accession number: A1RGN2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 52 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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