ECOLI:DNAJ

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dnaJ (synonyms: groP)
Protein Name(s)	Chaperone protein DnaJ HSP40 Heat shock protein J
External Links
UniProt	P08622
EMBL	M12544 M12565 U00096 AP009048
PIR	A92572
RefSeq	NP_414556.1 WP_001118476.1
PDB	1BQ0 1BQZ 1EXK 1XBL 5NRO
PDBsum	1BQ0 1BQZ 1EXK 1XBL 5NRO
ProteinModelPortal	P08622
SMR	P08622
BioGrid	4259725 849156
DIP	DIP-9460N
IntAct	P08622
MINT	P08622
STRING	316385.ECDH10B_0015
EPD	P08622
PaxDb	P08622
PRIDE	P08622
EnsemblBacteria	AAC73126 BAB96590
GeneID	944753
KEGG	ecj:JW0014 eco:b0015
PATRIC	fig\|1411691.4.peg.2269
EchoBASE	EB0236
EcoGene	EG10240
eggNOG	ENOG4105BZ5 COG0484
HOGENOM	HOG000226717
InParanoid	P08622
KO	K03686
OMA	DMGGFAD
PhylomeDB	P08622
BioCyc	EcoCyc:EG10240-MONOMER MetaCyc:EG10240-MONOMER
EvolutionaryTrace	P08622
PRO	PR:P08622
Proteomes	UP000000318 UP000000625
GO	GO:0005737 GO:0005829 GO:0016020 GO:0043234 GO:0005524 GO:0051087 GO:0031072 GO:0003756 GO:0015035 GO:0016989 GO:0051082 GO:0008270 GO:0051085 GO:0006260 GO:0006461 GO:0006457 GO:0042026 GO:0009408 GO:0016032
CDD	cd06257 cd10719
Gene3D	1.10.287.110
HAMAP	MF_01152
InterPro	IPR012724 IPR002939 IPR001623 IPR018253 IPR008971 IPR001305 IPR036410 IPR036869
Pfam	PF00226 PF01556 PF00684
PRINTS	PR00625
SMART	SM00271
SUPFAM	SSF46565 SSF49493 SSF57938
TIGRFAMs	TIGR02349
PROSITE	PS00636 PS50076 PS51188

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:9103205^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:9103205^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:9103205^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:9103205^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A6Y8	F	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:9103205^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10240 PANTHER:PTN002454318 TAIR:locus:2162692	P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10240 PANTHER:PTN002454318 SGD:S000001878	F	Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10240 PANTHER:PTN002454318 SGD:S000001878	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10240 PANTHER:PTN002454318 SGD:S000001878 TAIR:locus:2016234 TAIR:locus:2041258 TAIR:locus:2088585 TAIR:locus:2140035 TAIR:locus:2162692 TAIR:locus:2172374 UniProtKB:A0A1P8BB64 UniProtKB:Q583X4	C	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:7559385^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0042026	protein refolding	PMID:7559385^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:6220698^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:3889001^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:8349564^[6]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:12941935^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:8662861^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:11985624^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:7559385^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	PMID:2144273^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:6220698^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003756	protein disulfide isomerase activity	PMID:7559385^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:7900997^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016989	sigma factor antagonist activity	PMID:8599944^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	PMID:2144273^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	PMID:3889001^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	PMID:1361234^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0015035	protein disulfide oxidoreductase activity	PMID:11732919^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:2144273^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:6220698^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0015035	P	Seeded From UniProt	complete
involved_in	GO:1903507	negative regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0016989	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012724	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008971 InterPro:IPR012724	P	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012724	P	Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001305	F	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001305 InterPro:IPR008971 InterPro:IPR012724	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100773	C	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100773	F	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100773	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Harrison, CJ et al. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276 431-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 de Crouy-Chanel, A et al. (1995) A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase. J. Biol. Chem. 270 22669-72 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Zylicz, M et al. (1983) Escherichia coli dnaJ- and dnaK-gene products: synthesis in minicells and membrane-affinity. Biochem. Biophys. Res. Commun. 110 176-80 PubMed GONUTS page
↑ ^5.0 ^5.1 Zylicz, M et al. (1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J. Biol. Chem. 260 7591-8 PubMed GONUTS page
↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
↑ Linke, K et al. (2003) The roles of the two zinc binding sites in DnaJ. J. Biol. Chem. 278 44457-66 PubMed GONUTS page
↑ Banecki, B et al. (1996) Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone. J. Biol. Chem. 271 14840-8 PubMed GONUTS page
↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Sell, SM et al. (1990) Isolation and characterization of dnaJ null mutants of Escherichia coli. J. Bacteriol. 172 4827-35 PubMed GONUTS page
↑ Schröder, H et al. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12 4137-44 PubMed GONUTS page
↑ Gamer, J et al. (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15 607-17 PubMed GONUTS page
↑ Hoffmann, HJ et al. (1992) Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein. Proc. Natl. Acad. Sci. U.S.A. 89 12108-11 PubMed GONUTS page
↑ Tang, W & Wang, CC (2001) Zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ. Biochemistry 40 14985-94 PubMed GONUTS page

[PMID:9103205-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Harrison, CJ et al. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276 431-5 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:7559385-3] 3.0 ^3.1 ^3.2 ^3.3 de Crouy-Chanel, A et al. (1995) A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase. J. Biol. Chem. 270 22669-72 PubMed GONUTS page

[PMID:6220698-4] 4.0 ^4.1 ^4.2 Zylicz, M et al. (1983) Escherichia coli dnaJ- and dnaK-gene products: synthesis in minicells and membrane-affinity. Biochem. Biophys. Res. Commun. 110 176-80 PubMed GONUTS page

[PMID:3889001-5] 5.0 ^5.1 Zylicz, M et al. (1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J. Biol. Chem. 260 7591-8 PubMed GONUTS page

[PMID:8349564-6] Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page

[PMID:12941935-7] Linke, K et al. (2003) The roles of the two zinc binding sites in DnaJ. J. Biol. Chem. 278 44457-66 PubMed GONUTS page

[PMID:8662861-8] Banecki, B et al. (1996) Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone. J. Biol. Chem. 271 14840-8 PubMed GONUTS page

[PMID:11985624-9] Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed GONUTS page

[PMID:2144273-10] 10.0 ^10.1 ^10.2 Sell, SM et al. (1990) Isolation and characterization of dnaJ null mutants of Escherichia coli. J. Bacteriol. 172 4827-35 PubMed GONUTS page

[PMID:7900997-11] Schröder, H et al. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12 4137-44 PubMed GONUTS page

[PMID:8599944-12] Gamer, J et al. (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15 607-17 PubMed GONUTS page

[PMID:1361234-13] Hoffmann, HJ et al. (1992) Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein. Proc. Natl. Acad. Sci. U.S.A. 89 12108-11 PubMed GONUTS page

[PMID:11732919-14] Tang, W & Wang, CC (2001) Zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ. Biochemistry 40 14985-94 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

ECOLI:DNAJ

Contents

Annotations

Notes

References

a

b

c

d

e

g

h

m

o

p

r

s

u

v

z

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools