ECOLI:UVRD

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	uvrD (synonyms: mutU, pdeB, rad, recL)
Protein Name(s)	DNA helicase II
External Links
UniProt	P03018
EMBL	X00738 D00069 X04037 M87049 U00096 AP009048 X00225 M38257
PIR	F65185
RefSeq	NP_418258.1 YP_491628.1
PDB	2IS1 2IS2 2IS4 2IS6 3LFU
PDBsum	2IS1 2IS2 2IS4 2IS6 3LFU
DisProt	DP00684
ProteinModelPortal	P03018
SMR	P03018
DIP	DIP-11103N
IntAct	P03018
MINT	MINT-1223204
STRING	511145.b3813
PaxDb	P03018
PRIDE	P03018
EnsemblBacteria	AAC76816 BAE77487
GeneID	12934346 948347
KEGG	ecj:Y75_p3364 eco:b3813
PATRIC	32123127
EchoBASE	EB1057
EcoGene	EG11064
eggNOG	COG0210
HOGENOM	HOG000033016
InParanoid	P03018
KO	K03657
OMA	RLQIAFQ
OrthoDB	EOG64N9TW
PhylomeDB	P03018
BioCyc	EcoCyc:EG11064-MONOMER ECOL316407:JW3786-MONOMER MetaCyc:EG11064-MONOMER
EvolutionaryTrace	P03018
PRO	PR:P03018
Proteomes	UP000000318 UP000000625
Genevestigator	P03018
GO	GO:0005829 GO:0005524 GO:0003677 GO:0003678 GO:0015616 GO:0017116 GO:0006200 GO:0032508 GO:0006268 GO:0006298 GO:0006289 GO:0051260 GO:0031297 GO:0070581 GO:0009432
Gene3D	1.10.10.160 3.40.50.300
InterPro	IPR013986 IPR005753 IPR014017 IPR000212 IPR027417 IPR014016
PANTHER	PTHR11070
Pfam	PF00580 PF13361
SUPFAM	SSF52540
TIGRFAMs	TIGR01075
PROSITE	PS51198 PS51217

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0006260	DNA replication	PMID:19851282^[1]	ECO:0000315			P	Fig 4 and Fig 5	complete
	GO:0009411	response to UV	PMID:19762288^[2]	ECO:0000315			P	Figure five shows that strains with a functional copy of uvrD survive drastically better after exposure to UV light.	complete
	GO:0003678	DNA helicase activity	PMID:19762288^[2]	ECO:0000315			F	Figure six illustrates that strains lacking the uvrD gene have helicases with a lower affinity for single stranded DNA	complete
enables	GO:0003678	DNA helicase activity	PMID:2942537^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043140	ATP-dependent 3'-5' DNA helicase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10426 PANTHER:PTN000116141 SGD:S000005455 UniProtKB:A0A1D8PUB1 UniProtKB:P9WMQ1 UniProtKB:Q8I3W6	F	Seeded From UniProt	complete
part_of	GO:0033202	DNA helicase complex	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000116196 UniProtKB:P9WMQ1	C	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11064 PANTHER:PTN000116141 PomBase:SPAC4H3.05 PomBase:SPBC336.01 SGD:S000003628 UniProtKB:F1ND48 UniProtKB:G3XD04 UniProtKB:P9WMQ1	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10426 EcoGene:EG11064 PANTHER:PTN000869814 UniProtKB:P9WMQ3	C	Seeded From UniProt	complete
involved_in	GO:0000725	recombinational repair	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000116141 PomBase:SPAC4H3.05 PomBase:SPBC336.01 UniProtKB:F1ND48	P	Seeded From UniProt	complete
involved_in	GO:0070581	rolling circle DNA replication	PMID:10632890^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:23442971^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
	GO:0003678	DNA helicase activity	PMID:2942537^[3]	ECO:0000314			F	Figure 3 shows that Helicase II translocates along single-stranded DNA in the 3' to 5' direction	complete CACAO 2039
involved_in	GO:0051260	protein homooligomerization	PMID:10543970^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
	GO:0043138	3'-5' DNA helicase activity	PMID:2942537^[3]	ECO:0000314			F	Figure 3 shows that Helicase II translocates along single-stranded DNA in the 3' to 5' direction	complete
involved_in	GO:0032508	DNA duplex unwinding	PMID:2942537^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031297	replication fork processing	PMID:15375374^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0017116	single-stranded DNA-dependent ATP-dependent DNA helicase activity	PMID:6135974^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0017116	single-stranded DNA-dependent ATP-dependent DNA helicase activity	PMID:2942537^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0017116	single-stranded DNA-dependent ATP-dependent DNA helicase activity	PMID:25883359^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0015616	DNA translocase activity	PMID:2942537^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0015616	DNA translocase activity	PMID:25883359^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006298	mismatch repair	PMID:6308634^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:24402227^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	PMID:1530937^[14]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:6135974^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000212	F	Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000212 InterPro:IPR005753	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:IPR000212 InterPro:IPR014016 InterPro:IPR014017 InterPro:IPR034739	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005753	C	Seeded From UniProt	complete
involved_in	GO:0006268	DNA unwinding involved in DNA replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005753	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014017	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
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
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	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
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	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
involved_in	GO:0009432	SOS response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0742	P	Seeded From UniProt	complete
edit table

Notes

References

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

↑ Boubakri, H et al. (2010) The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo. EMBO J. 29 145-57 PubMed GONUTS page
↑ ^2.0 ^2.1 Manelyte, L et al. (2009) The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair. DNA Repair (Amst.) 8 1300-10 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Matson, SW (1986) Escherichia coli helicase II (urvD gene product) translocates unidirectionally in a 3' to 5' direction. J. Biol. Chem. 261 10169-75 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Bruand, C & Ehrlich, SD (2000) UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Mol. Microbiol. 35 204-10 PubMed GONUTS page
↑ Yokota, H et al. (2013) Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase. Biophys. J. 104 924-33 PubMed GONUTS page
↑ Ali, JA et al. (1999) An oligomeric form of E. coli UvrD is required for optimal helicase activity. J. Mol. Biol. 293 815-34 PubMed GONUTS page
↑ Flores, MJ et al. (2004) The DNA repair helicase UvrD is essential for replication fork reversal in replication mutants. EMBO Rep. 5 983-8 PubMed GONUTS page
↑ ^9.0 ^9.1 Hickson, ID et al. (1983) The E. coli uvrD gene product is DNA helicase II. Mol. Gen. Genet. 190 265-70 PubMed GONUTS page
↑ ^10.0 ^10.1 Comstock, MJ et al. (2015) Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme. Science 348 352-4 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Lu, AL et al. (1983) Methyl-directed repair of DNA base-pair mismatches in vitro. Proc. Natl. Acad. Sci. U.S.A. 80 4639-43 PubMed GONUTS page
↑ Epshtein, V et al. (2014) UvrD facilitates DNA repair by pulling RNA polymerase backwards. Nature 505 372-7 PubMed GONUTS page
↑ Orren, DK et al. (1992) Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I. J. Biol. Chem. 267 780-8 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:19851282-1] Boubakri, H et al. (2010) The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo. EMBO J. 29 145-57 PubMed GONUTS page

[PMID:19762288-2] 2.0 ^2.1 Manelyte, L et al. (2009) The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair. DNA Repair (Amst.) 8 1300-10 PubMed GONUTS page

[PMID:2942537-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Matson, SW (1986) Escherichia coli helicase II (urvD gene product) translocates unidirectionally in a 3' to 5' direction. J. Biol. Chem. 261 10169-75 PubMed GONUTS page

[PMID:21873635-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 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:10632890-5] Bruand, C & Ehrlich, SD (2000) UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Mol. Microbiol. 35 204-10 PubMed GONUTS page

[PMID:23442971-6] Yokota, H et al. (2013) Single-molecule imaging of the oligomer formation of the nonhexameric Escherichia coli UvrD helicase. Biophys. J. 104 924-33 PubMed GONUTS page

[PMID:10543970-7] Ali, JA et al. (1999) An oligomeric form of E. coli UvrD is required for optimal helicase activity. J. Mol. Biol. 293 815-34 PubMed GONUTS page

[PMID:15375374-8] Flores, MJ et al. (2004) The DNA repair helicase UvrD is essential for replication fork reversal in replication mutants. EMBO Rep. 5 983-8 PubMed GONUTS page

[PMID:6135974-9] 9.0 ^9.1 Hickson, ID et al. (1983) The E. coli uvrD gene product is DNA helicase II. Mol. Gen. Genet. 190 265-70 PubMed GONUTS page

[PMID:25883359-10] 10.0 ^10.1 Comstock, MJ et al. (2015) Protein structure. Direct observation of structure-function relationship in a nucleic acid-processing enzyme. Science 348 352-4 PubMed GONUTS page

[PMID:27718375-11] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:6308634-12] Lu, AL et al. (1983) Methyl-directed repair of DNA base-pair mismatches in vitro. Proc. Natl. Acad. Sci. U.S.A. 80 4639-43 PubMed GONUTS page

[PMID:24402227-13] Epshtein, V et al. (2014) UvrD facilitates DNA repair by pulling RNA polymerase backwards. Nature 505 372-7 PubMed GONUTS page

[PMID:1530937-14] Orren, DK et al. (1992) Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I. J. Biol. Chem. 267 780-8 PubMed GONUTS page

[PMID:18304323-15] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

ECOLI:UVRD

Contents

Annotations

Notes

References

3

a

b

c

d

e

g

h

m

n

p

r

s

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools