ECOLI:UMUD

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	umuD
Protein Name(s)	Protein UmuD Protein UmuD'
External Links
UniProt	P0AG11
EMBL	M10107 M13387 U00096 AP009048
PIR	A03551
RefSeq	NP_415701.1 YP_489450.1
PDB	1AY9 1I4V 1UMU
PDBsum	1AY9 1I4V 1UMU
DisProt	DP00626
ProteinModelPortal	P0AG11
SMR	P0AG11
DIP	DIP-29679N
IntAct	P0AG11
STRING	511145.b1183
MEROPS	S24.003
EnsemblBacteria	AAC74267 BAA36030
GeneID	12932823 945746
KEGG	ecj:Y75_p1155 eco:b1183
PATRIC	32117612
EchoBASE	EB1050
EcoGene	EG11057
eggNOG	COG1974
HOGENOM	HOG000232166
InParanoid	P0AG11
KO	K03503
OMA	FMERVSA
OrthoDB	EOG6JHRHJ
PhylomeDB	P0AG11
BioCyc	EcoCyc:EG11057-MONOMER ECOL316407:JW1172-MONOMER MetaCyc:EG11057-MONOMER
EvolutionaryTrace	P0AG11
PRO	PR:P0AG11
Proteomes	UP000000318 UP000000625
Genevestigator	P0AG11
GO	GO:0003677 GO:0003887 GO:0008236 GO:0006974 GO:0071897 GO:0006281 GO:0006355 GO:0009432
Gene3D	2.10.109.10
InterPro	IPR028360 IPR006197 IPR019759 IPR015927
Pfam	PF00717
PRINTS	PR00726
SUPFAM	SSF51306

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0042802	identical protein binding	PMID:9406544^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AG11	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:8614470^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AG11	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18216271^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AG11	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:10760165^[4]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019985	translesion synthesis	PMID:10542196^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019985	translesion synthesis	PMID:10430871^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	PMID:10760155^[7]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0009355	DNA polymerase V complex	PMID:10542196^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0009355	DNA polymerase V complex	PMID:10430871^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	PMID:24843026^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:10760155^[7]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:10648540^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003887	DNA-directed DNA polymerase activity	PMID:12450411^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:8631887^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006197	F	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006197	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: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
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	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
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
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt	complete
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Notes

References

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

↑ Ferentz, AE et al. (1997) Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis. Nat. Struct. Biol. 4 979-83 PubMed GONUTS page
↑ Peat, TS et al. (1996) Structure of the UmuD' protein and its regulation in response to DNA damage. Nature 380 727-30 PubMed GONUTS page
↑ Simon, SM et al. (2008) Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. Proc. Natl. Acad. Sci. U.S.A. 105 1152-7 PubMed GONUTS page
↑ Caramel, A & Schnetz, K (2000) Antagonistic control of the Escherichia coli bgl promoter by FIS and CAP in vitro. Mol. Microbiol. 36 85-92 PubMed GONUTS page
↑ ^5.0 ^5.1 Reuven, NB et al. (1999) The mutagenesis protein UmuC is a DNA polymerase activated by UmuD', RecA, and SSB and is specialized for translesion replication. J. Biol. Chem. 274 31763-6 PubMed GONUTS page
↑ ^6.0 ^6.1 Tang, M et al. (1999) UmuD'(2)C is an error-prone DNA polymerase, Escherichia coli pol V. Proc. Natl. Acad. Sci. U.S.A. 96 8919-24 PubMed GONUTS page
↑ ^7.0 ^7.1 Fernández De Henestrosa, AR et al. (2000) Identification of additional genes belonging to the LexA regulon in Escherichia coli. Mol. Microbiol. 35 1560-72 PubMed GONUTS page
↑ Erdem, AL et al. (2014) DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase. Elife 3 e02384 PubMed GONUTS page
↑ Murli, S et al. (2000) A role for the umuDC gene products of Escherichia coli in increasing resistance to DNA damage in stationary phase by inhibiting the transition to exponential growth. J. Bacteriol. 182 1127-35 PubMed GONUTS page
↑ Maor-Shoshani, A & Livneh, Z (2002) Analysis of the stimulation of DNA polymerase V of Escherichia coli by processivity proteins. Biochemistry 41 14438-46 PubMed GONUTS page
↑ Bruck, I et al. (1996) Purification of a soluble UmuD'C complex from Escherichia coli. Cooperative binding of UmuD'C to single-stranded DNA. J. Biol. Chem. 271 10767-74 PubMed GONUTS page

[PMID:9406544-1] Ferentz, AE et al. (1997) Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis. Nat. Struct. Biol. 4 979-83 PubMed GONUTS page

[PMID:8614470-2] Peat, TS et al. (1996) Structure of the UmuD' protein and its regulation in response to DNA damage. Nature 380 727-30 PubMed GONUTS page

[PMID:18216271-3] Simon, SM et al. (2008) Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. Proc. Natl. Acad. Sci. U.S.A. 105 1152-7 PubMed GONUTS page

[PMID:10760165-4] Caramel, A & Schnetz, K (2000) Antagonistic control of the Escherichia coli bgl promoter by FIS and CAP in vitro. Mol. Microbiol. 36 85-92 PubMed GONUTS page

[PMID:10542196-5] 5.0 ^5.1 Reuven, NB et al. (1999) The mutagenesis protein UmuC is a DNA polymerase activated by UmuD', RecA, and SSB and is specialized for translesion replication. J. Biol. Chem. 274 31763-6 PubMed GONUTS page

[PMID:10430871-6] 6.0 ^6.1 Tang, M et al. (1999) UmuD'(2)C is an error-prone DNA polymerase, Escherichia coli pol V. Proc. Natl. Acad. Sci. U.S.A. 96 8919-24 PubMed GONUTS page

[PMID:10760155-7] 7.0 ^7.1 Fernández De Henestrosa, AR et al. (2000) Identification of additional genes belonging to the LexA regulon in Escherichia coli. Mol. Microbiol. 35 1560-72 PubMed GONUTS page

[PMID:24843026-8] Erdem, AL et al. (2014) DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase. Elife 3 e02384 PubMed GONUTS page

[PMID:10648540-9] Murli, S et al. (2000) A role for the umuDC gene products of Escherichia coli in increasing resistance to DNA damage in stationary phase by inhibiting the transition to exponential growth. J. Bacteriol. 182 1127-35 PubMed GONUTS page

[PMID:12450411-10] Maor-Shoshani, A & Livneh, Z (2002) Analysis of the stimulation of DNA polymerase V of Escherichia coli by processivity proteins. Biochemistry 41 14438-46 PubMed GONUTS page

[PMID:8631887-11] Bruck, I et al. (1996) Purification of a soluble UmuD'C complex from Escherichia coli. Cooperative binding of UmuD'C to single-stranded DNA. J. Biol. Chem. 271 10767-74 PubMed GONUTS page

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ECOLI:UMUD

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