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P63971 (DNAJ_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:SA1408
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 MF_01152

Cofactor

Binds 2 zinc ions per monomer By similarity. HAMAP MF_01152

Subunit structure

Homodimer By similarity. HAMAP MF_01152

Subcellular location

Cytoplasm By similarity HAMAP 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 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

heat shock protein binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Chaperone protein DnaJ HAMAP MF_01152
PRO_0000070884

Regions

Domain5 – 6965J
Repeat149 – 1568CXXCXGXG motif HAMAP MF_01152
Repeat166 – 1738CXXCXGXG motif HAMAP MF_01152
Repeat192 – 1998CXXCXGXG motif HAMAP MF_01152
Repeat206 – 2138CXXCXGXG motif HAMAP MF_01152
Zinc finger136 – 21883CR-type HAMAP MF_01152
Compositional bias74 – 11946Gly-rich HAMAP MF_01152

Sites

Metal binding1491Zinc 1 By similarity
Metal binding1521Zinc 1 By similarity
Metal binding1661Zinc 2 By similarity
Metal binding1691Zinc 2 By similarity
Metal binding1921Zinc 2 By similarity
Metal binding1951Zinc 2 By similarity
Metal binding2061Zinc 1 By similarity
Metal binding2091Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
P63971 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 1D6C22CBFF511E5B

FASTA37941,761
        10         20         30         40         50         60 
MAKRDYYEVL GISKDASKDE IKKAYRKLSK KYHPDINKEE GADEKFKEIS EAYEVLSDDN 

        70         80         90        100        110        120 
KRASYDQFGH DGPQGFGGQG FNGSDFGGFS GFGGGGFEDI FSSFFGGGRQ RDPNAPQKGD 

       130        140        150        160        170        180 
DLQYTMTLTF EEAVFGTTKE ISIRKDVTCE TCHGDGAKPG TSKKTCSYCN GAGHVAVEQN 

       190        200        210        220        230        240 
TILGRVRTEQ VCPKCNGSGQ EFEEACPTCH GKGTENKTVK LEVKVPEGVD NEQQIRLAGE 

       250        260        270        280        290        300 
GSPGVNGGPA GDLYVVFRVK PSETFKRDGD DIYYKLNVSF PQAALGDEIK IPTLNNEVML 

       310        320        330        340        350        360 
TIPAGTQTGK QFRLKEKGIK NVHGYGYGDL YVDIKVVTPT KLTDRQKELM KEFAQLNGEE 

       370 
INEQPSNFKD RAKRFFKGE 

« Hide

References

[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB42671.1.
PIRB89939.
RefSeqNP_374692.1. NC_002745.2.

3D structure databases

ProteinModelPortalP63971.
SMRP63971. Positions 2-70.
ModBaseSearch...

Protein-protein interaction databases

STRINGP63971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000000617; EBSTAP00000000617; EBSTAG00000000617.
GeneID1124249.
GenomeReviewsGene locus SA1408 in contig BA000018_GR.
KEGGsau:SA1408.
PATRIC19575090. VBIStaAur116463_1514.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0484.
GeneTreeEBGT00050000024869.
HOGENOMHBG635315.
OMAENKRANY.
PhylomeDBP63971.
ProtClustDBPRK14280.

Enzyme and pathway databases

BioCycSAUR158879:SA1408-MONOMER.

Family and domain databases

HAMAPMF_01152. DnaJ.
[Tree]
InterProIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_N.
IPR018253. Heat_shock_DnaJ_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR003095. Hsp_DnaJ.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
Gene3DG3DSA:1.10.287.110. DnaJ_N. 1 hit.
G3DSA:2.10.230.10. HSP_DnaJ_cys-rich. 1 hit.
KOK03686.
PANTHERPTHR24076:SF80. PTHR24076:SF80. 1 hit.
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_STAAN
AccessionPrimary (citable) accession number: P63971
Secondary accession number(s): Q99TR8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 57 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