Q8XA65 (DNAJ_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chaperone protein DnaJ

Gene names

Name:	dnaJ
Ordered Locus Names:	Z0015, ECs0015

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.
Induction	By heat shock 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 process	DNA replication Stress response
Cellular component	Cytoplasm
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chaperone
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA 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_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 376	375	Chaperone protein DnaJ HAMAP-Rule MF_01152		PRO_0000070778
Regions
	Domain	5 – 70	66	J
	Repeat	144 – 151	8	CXXCXGXG motif HAMAP-Rule MF_01152
	Repeat	161 – 168	8	CXXCXGXG motif HAMAP-Rule MF_01152
	Repeat	183 – 190	8	CXXCXGXG motif HAMAP-Rule MF_01152
	Repeat	197 – 204	8	CXXCXGXG motif HAMAP-Rule MF_01152
	Zinc finger	131 – 209	79	CR-type HAMAP-Rule MF_01152
	Compositional bias	77 – 114	38	Gly-rich HAMAP-Rule MF_01152
Sites
	Metal binding	144	1	Zinc 1 By similarity
	Metal binding	147	1	Zinc 1 By similarity
	Metal binding	161	1	Zinc 2 By similarity
	Metal binding	164	1	Zinc 2 By similarity
	Metal binding	183	1	Zinc 2 By similarity
	Metal binding	186	1	Zinc 2 By similarity
	Metal binding	197	1	Zinc 1 By similarity
	Metal binding	200	1	Zinc 1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XA65 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8B7ADC315B7E6F4A	FASTA	376	41,044
	10 20 30 40 50 60 MAKQDYYEIL GVSKTAEERE IKKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS 70 80 90 100 110 120 QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN 130 140 150 160 170 180 MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ 190 200 210 220 230 240 QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP 250 260 270 280 290 300 AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG 310 320 330 340 350 360 KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNEKQKQL LQELQESFGG PTGEHNSPRS 370 KSFFDGVKKF FDDLTR

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG54315.1. BA000007 Genomic DNA. Translation: BAB33438.1.
PIR	G85481. G90630.
RefSeq	NP_285707.1. NC_002655.2. NP_308042.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8XA65.
SMR	Q8XA65. Positions 2-78, 131-350.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z0015.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG54315; AAG54315; Z0015. BAB33438; BAB33438; BAB33438.
GeneID	913407. 956674.
KEGG	ece:Z0015. ecs:ECs0015.
PATRIC	18348966. VBIEscCol44059_0013.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0484.
HOGENOM	HOG000226717.
KO	K03686.
OMA	HCHGRGK.
ProtClustDB	PRK10767.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-14-MONOMER.
Family and domain databases
Gene3D	1.10.287.110. 1 hit. 2.10.230.10. 1 hit.
HAMAP	MF_01152. DnaJ.
InterPro	IPR012724. DnaJ. IPR002939. DnaJ_C. IPR001623. DnaJ_domain. IPR018253. DnaJ_domain_CS. IPR008971. HSP40/DnaJ_pept-bd. IPR001305. HSP_DnaJ_Cys-rich_dom. [Graphical view]
Pfam	PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. PF00684. DnaJ_CXXCXGXG. 1 hit. [Graphical view]
PRINTS	PR00625. JDOMAIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit. SSF49493. HSP40_DnaJ_pep. 2 hits. SSF57938. HSP_DnaJ_cys-rich. 1 hit.
TIGRFAMs	TIGR02349. DnaJ_bact. 1 hit.
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. PS51188. ZF_CR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNAJ_ECO57

Accession

Primary (citable) accession number: Q8XA65
Secondary accession number(s): Q7AHU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program