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Q92J37 (DNAJ_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:RC0232
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length373 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

nucleic acid 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 – 373373Chaperone protein DnaJ HAMAP-Rule MF_01152
PRO_0000070871

Regions

Domain4 – 6865J
Repeat149 – 1568CXXCXGXG motif HAMAP-Rule MF_01152
Repeat166 – 1738CXXCXGXG motif HAMAP-Rule MF_01152
Repeat188 – 1958CXXCXGXG motif HAMAP-Rule MF_01152
Repeat202 – 2098CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger136 – 21479CR-type HAMAP-Rule MF_01152
Compositional bias75 – 11945Gly-rich HAMAP-Rule MF_01152

Sites

Metal binding1491Zinc 1 By similarity
Metal binding1521Zinc 1 By similarity
Metal binding1661Zinc 2 By similarity
Metal binding1691Zinc 2 By similarity
Metal binding1881Zinc 2 By similarity
Metal binding1911Zinc 2 By similarity
Metal binding2021Zinc 1 By similarity
Metal binding2051Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92J37 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1A0C23B6E0A2A54D

FASTA37341,131
        10         20         30         40         50         60 
MSQNYYQILG VSKTASQADL KKAYLKLAKQ YHPDTTDAKD AEKKFKEINA AYDVLKDEQK 

        70         80         90        100        110        120 
RAAYDRLGHD AFQNQQSRGG GGNHGGFHPD INDIFGDFFS DFMGGSRRSS RPTSAKVRGS 

       130        140        150        160        170        180 
DLKYNLTINL EEAFHGIEKN ISFSSAVKCD TCHGSGSEKG ETVTTCDACS GVGATRMQQG 

       190        200        210        220        230        240 
FFTIEQACHK CQGNGHIIKN PCKKCHGMGR YHKQRNLSVN IPAGVENGTR IRHTGEGEAG 

       250        260        270        280        290        300 
IRGGNSGDLY VDITIKPHDI YKVDGANLHC KLPISFVNAA LGGEIEVPVI EGGKVNLTIP 

       310        320        330        340        350        360 
AGTQNGDQLR LRSKGMSKMR STIRGDMLTH IHVEVPKNLS KRQRELLEEF KKESINEKEN 

       370 
DGSFFNKMKS LWS 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02770.1.
PIRH97728.
RefSeqNP_359869.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92J37.
SMRQ92J37. Positions 3-73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02770; AAL02770; RC0232.
GeneID927956.
KEGGrco:RC0232.
PATRIC17887617. VBIRicCon45613_0268.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226717.
KOK03686.
OMAGHTDPNQ.
OrthoDBEOG6BPDKP.

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.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
SM00343. ZnF_C2HC. 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_RICCN
AccessionPrimary (citable) accession number: Q92J37
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 81 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

Rickettsia conorii

(strain Malish 7): entries and gene names