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Protein

Chaperone protein DnaJ

Gene

dnaJ

Organism
Peptoclostridium difficile (strain 630) (Clostridium difficile)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Zinc 1UniRule annotation
Metal bindingi157 – 1571Zinc 1UniRule annotation
Metal bindingi171 – 1711Zinc 2UniRule annotation
Metal bindingi174 – 1741Zinc 2UniRule annotation
Metal bindingi197 – 1971Zinc 2UniRule annotation
Metal bindingi200 – 2001Zinc 2UniRule annotation
Metal bindingi211 – 2111Zinc 1UniRule annotation
Metal bindingi214 – 2141Zinc 1UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri141 – 22383CR-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

DNA replication, Stress response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciCDIF272563:GJFE-2678-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein DnaJUniRule annotation
Gene namesi
Name:dnaJUniRule annotation
Ordered Locus Names:CD630_24600
OrganismiPeptoclostridium difficile (strain 630) (Clostridium difficile)
Taxonomic identifieri272563 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium
Proteomesi
  • UP000001978 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384Chaperone protein DnaJPRO_1000085177Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272563.CD2460.

Structurei

3D structure databases

ProteinModelPortaliQ182E7.
SMRiQ182E7. Positions 4-72.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 7166JUniRule annotationAdd
BLAST
Repeati154 – 1618CXXCXGXG motif
Repeati171 – 1788CXXCXGXG motif
Repeati197 – 2048CXXCXGXG motif
Repeati211 – 2188CXXCXGXG motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi78 – 12447Gly-richAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the DnaJ family.UniRule annotation
Contains 1 CR-type zinc finger.UniRule annotation
Contains 1 J domain.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri141 – 22383CR-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG4105BZ5. Bacteria.
COG0484. LUCA.
HOGENOMiHOG000226717.
KOiK03686.
OMAiDEGMRIR.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ. 1 hit.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
TIGRFAMsiTIGR02349. DnaJ_bact. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q182E7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKRDYYEV LGISKGAEAQ EIKKAYRKLA MKYHPDRNPG DKEAEEKFKE
60 70 80 90 100
INEAYEVLSD DTKRKTYDQF GHDGLNGQGG FGGQGGFGGQ GFGGFEDMFG
110 120 130 140 150
DIFGDMFGGS FGGGRARRRG PQRGADIRQS VTISFEEAAF GKKMSIKVNR
160 170 180 190 200
SEECEECNGT GAKPGTSKKT CSTCNGTGQV RTVQRTPFGN IASSRPCSAC
210 220 230 240 250
NGTGEVIESP CSKCHGTGNT RKVKTIEVDI PAGIDDGQMI KLSGQGEVGE
260 270 280 290 300
KGAPRGDLYI VVNVKSHPLF TRDGNDIYFE MPITFVQATL GDEIEVPTLD
310 320 330 340 350
GKVKYSVPEG TQTGTVFRLK EKGIPRIRGN SRGDQYVKVV VEIPKKLNDK
360 370 380
QKELLREFAK ECGSNVHEKK KTFGQKIEDM FKKK
Length:384
Mass (Da):42,071
Last modified:July 25, 2006 - v1
Checksum:i4DD692661CB6F2B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ69347.1.
RefSeqiWP_004454751.1. NZ_CP010905.1.
YP_001088974.1. NC_009089.1.

Genome annotation databases

EnsemblBacteriaiCAJ69347; CAJ69347; CD630_24600.
GeneIDi4916450.
KEGGicdf:CD630_24600.
pdc:CDIF630_02706.
PATRICi19443391. VBICloDif38397_2582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ69347.1.
RefSeqiWP_004454751.1. NZ_CP010905.1.
YP_001088974.1. NC_009089.1.

3D structure databases

ProteinModelPortaliQ182E7.
SMRiQ182E7. Positions 4-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272563.CD2460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ69347; CAJ69347; CD630_24600.
GeneIDi4916450.
KEGGicdf:CD630_24600.
pdc:CDIF630_02706.
PATRICi19443391. VBICloDif38397_2582.

Phylogenomic databases

eggNOGiENOG4105BZ5. Bacteria.
COG0484. LUCA.
HOGENOMiHOG000226717.
KOiK03686.
OMAiDEGMRIR.

Enzyme and pathway databases

BioCyciCDIF272563:GJFE-2678-MONOMER.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ. 1 hit.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
TIGRFAMsiTIGR02349. DnaJ_bact. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNAJ_PEPD6
AccessioniPrimary (citable) accession number: Q182E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 25, 2006
Last modified: September 7, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.