ECOLI:DBPA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	dbpA (ECO:0000255 with HAMAP-Rule:MF_00965)
Protein Name(s)	ATP-dependent RNA helicase DbpA (ECO:0000255 with HAMAP-Rule:MF_00965)
External Links
UniProt	P21693
EMBL	X52647 U00096 AP009048
PIR	B64884
RefSeq	NP_415859.1 YP_489613.1
ProteinModelPortal	P21693
SMR	P21693
IntAct	P21693
STRING	511145.b1343
PaxDb	P21693
PRIDE	P21693
EnsemblBacteria	AAC74425 BAA14946
GeneID	12933991 947153
KEGG	ecj:Y75_p1320 eco:b1343
PATRIC	32117966
EchoBASE	EB0206
EcoGene	EG10210
eggNOG	COG0513
HOGENOM	HOG000268809
InParanoid	P21693
KO	K05591
OMA	KITVHPA
OrthoDB	EOG6GBMBM
PhylomeDB	P21693
BioCyc	EcoCyc:EG10210-MONOMER ECOL316407:JW1337-MONOMER MetaCyc:EG10210-MONOMER
PRO	PR:P21693
Proteomes	UP000000318 UP000000625
Genevestigator	P21693
GO	GO:0005737 GO:0043531 GO:0005524 GO:0034459 GO:0016887 GO:0033677 GO:0003724 GO:0019843 GO:0006200 GO:0008152 GO:0000027
Gene3D	3.40.50.300
HAMAP	MF_00965
InterPro	IPR005580 IPR011545 IPR028619 IPR014001 IPR001650 IPR027417 IPR000629 IPR014014
Pfam	PF03880 PF00270 PF00271
SMART	SM00487 SM00490
SUPFAM	SSF52540
PROSITE	PS00039 PS51192 PS51194 PS51195

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0033677	DNA/RNA helicase activity	PMID:9016593^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:9016593^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003724	RNA helicase activity	PMID:9016593^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043531	ADP binding	PMID:15654752^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0034459	ATP-dependent 3'-5' RNA helicase activity	PMID:15910005^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019843	rRNA binding	PMID:11888286^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:15654752^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000027	ribosomal large subunit assembly	PMID:19734347^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000027	ribosomal large subunit assembly	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028619	P	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011545	F	Seeded From UniProt	complete
enables	GO:0003724	RNA helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028619	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011545	F	Seeded From UniProt	complete
enables	GO:0034459	ATP-dependent 3'-5' RNA helicase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000111452	F	Seeded From UniProt	complete
involved_in	GO:0000027	ribosomal large subunit assembly	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000111452	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000111452	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000111452	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:UR000111452	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	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:0042254	ribosome biogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0690	P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Böddeker, N et al. (1997) Characterization of DbpA, an Escherichia coli DEAD box protein with ATP independent RNA unwinding activity. Nucleic Acids Res. 25 537-45 PubMed GONUTS page
↑ ^2.0 ^2.1 Talavera, MA & De La Cruz, EM (2005) Equilibrium and kinetic analysis of nucleotide binding to the DEAD-box RNA helicase DbpA. Biochemistry 44 959-70 PubMed GONUTS page
↑ Diges, CM & Uhlenbeck, OC (2005) Escherichia coli DbpA is a 3' --> 5' RNA helicase. Biochemistry 44 7903-11 PubMed GONUTS page
↑ Polach, KJ & Uhlenbeck, OC (2002) Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry 41 3693-702 PubMed GONUTS page
↑ Sharpe Elles, LM et al. (2009) A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit. Nucleic Acids Res. 37 6503-14 PubMed GONUTS page

[PMID:9016593-1] 1.0 ^1.1 ^1.2 Böddeker, N et al. (1997) Characterization of DbpA, an Escherichia coli DEAD box protein with ATP independent RNA unwinding activity. Nucleic Acids Res. 25 537-45 PubMed GONUTS page

[PMID:15654752-2] 2.0 ^2.1 Talavera, MA & De La Cruz, EM (2005) Equilibrium and kinetic analysis of nucleotide binding to the DEAD-box RNA helicase DbpA. Biochemistry 44 959-70 PubMed GONUTS page

[PMID:15910005-3] Diges, CM & Uhlenbeck, OC (2005) Escherichia coli DbpA is a 3' --> 5' RNA helicase. Biochemistry 44 7903-11 PubMed GONUTS page

[PMID:11888286-4] Polach, KJ & Uhlenbeck, OC (2002) Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry 41 3693-702 PubMed GONUTS page

[PMID:19734347-5] Sharpe Elles, LM et al. (2009) A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit. Nucleic Acids Res. 37 6503-14 PubMed GONUTS page

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ECOLI:DBPA

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