ECOLI:LEXA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	lexA (ECO:0000255 with HAMAP-Rule:MF_00015) (synonyms: exrA, spr, tsl, umuA)
Protein Name(s)	LexA repressor (ECO:0000255 with HAMAP-Rule:MF_00015)
External Links
UniProt	P0A7C2
EMBL	J01643 U00006 U00096 AP009048 L02362
PIR	A90808
RefSeq	NP_418467.1 YP_492186.1
PDB	1JHC 1JHE 1JHF 1JHH 1LEA 1LEB 1MVD 1QAA 3JSO 3JSP 3K3R
PDBsum	1JHC 1JHE 1JHF 1JHH 1LEA 1LEB 1MVD 1QAA 3JSO 3JSP 3K3R
ProteinModelPortal	P0A7C2
SMR	P0A7C2
DIP	DIP-51082N
IntAct	P0A7C2
MINT	MINT-1314348
STRING	511145.b4043
MEROPS	S24.001
PaxDb	P0A7C2
PRIDE	P0A7C2
EnsemblBacteria	AAC77013 BAE78045
GeneID	12932724 948544
KEGG	ecj:Y75_p3930 eco:b4043
PATRIC	32123623
EchoBASE	EB0528
EcoGene	EG10533
eggNOG	COG1974
HOGENOM	HOG000232167
InParanoid	P0A7C2
KO	K01356
OMA	IAETGMP
OrthoDB	EOG6JHRHJ
PhylomeDB	P0A7C2
BioCyc	EcoCyc:PD00205 ECOL316407:JW4003-MONOMER
EvolutionaryTrace	P0A7C2
PRO	PR:P0A7C2
Proteomes	UP000000318 UP000000625
Genevestigator	P0A7C2
GO	GO:0003677 GO:0004252 GO:0006974 GO:0006281 GO:0006260 GO:0045892 GO:0009432 GO:0006351
Gene3D	1.10.10.10 2.10.109.10
HAMAP	MF_00015
InterPro	IPR006200 IPR006199 IPR028360 IPR006197 IPR019759 IPR015927 IPR011991
Pfam	PF01726 PF00717
PRINTS	PR00726
SUPFAM	SSF51306
TIGRFAMs	TIGR00498

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0016481	negative regulation of transcription	PMID:368030^[1]	ECO:0000315			1	Figure 2 and Figure 3	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:10760155^[2]	ECO:0005653	northern assay evidence used in manual assertion		P	Seeded From UniProt	complete
Contributes to	GO:0009432	SOS response	PMID:21912525^[3]	ECO:0000314			P	Figure 3:RecA extended interface patch residues are involved in RecA active filament formation. The bacterial recombinase protein RecA is pivotal to DNA repair [1]–[4] and to orchestrate the bacterial DNA damage response (SOS response) against natural, or drug-induced, genotoxic conditions.	complete
Contributes to	GO:0009432		PMID:21912525^[3]	ECO:0000315				Figure 3:RecA extended interface patch residues are involved in RecA active filament formation. The bacterial recombinase protein RecA is pivotal to DNA repair [1]–[4] and to orchestrate the bacterial DNA damage response (SOS response) against natural, or drug-induced, genotoxic conditions.	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:21529368^[4]	ECO:0001808	reverse transcription polymerase chain reaction evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:19210620^[5]	ECO:0001808	reverse transcription polymerase chain reaction evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:10760155^[2]	ECO:0005643	hydroxyl-radical footprinting evidence used in manual assertion	RefSeq:NC_000913.2	C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:21529368^[4]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:19210620^[5]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:10760155^[2]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:10760155^[2]	ECO:0005643	hydroxyl-radical footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:21529368^[4]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:19210620^[5]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:10760155^[2]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:10760155^[2]	ECO:0005643	hydroxyl-radical footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:21529368^[4]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:19210620^[5]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:10760155^[2]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24561554^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A7C2	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20703307^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A7C2	F	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:10760155^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	PMID:4343824^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:2834329^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:10760155^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	PMID:3542969^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:160562^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:7027256^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	PMID:7027255^[13]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[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:IPR006197	F	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006199 InterPro:IPR006200	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
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006199	P	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006200	P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006200	P	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	P	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	F	Seeded From UniProt	complete
involved_in	GO:0009432	SOS response	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	P	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	P	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000075652	P	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: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: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
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
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: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
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Notes

References

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

↑ Pacelli, LZ et al. (1979) Isolation and characterization of amber mutations in the lexA gene of Escherichia coli K-12. J. Bacteriol. 137 568-73 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 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
↑ ^3.0 ^3.1 Adikesavan, AK et al. (2011) Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites. PLoS Genet. 7 e1002244 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Cambray, G et al. (2011) Prevalence of SOS-mediated control of integron integrase expression as an adaptive trait of chromosomal and mobile integrons. Mob DNA 2 6 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Prysak, MH et al. (2009) Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage. Mol. Microbiol. 71 1071-87 PubMed GONUTS page
↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
↑ Zhang, AP et al. (2010) Structure of the LexA-DNA complex and implications for SOS box measurement. Nature 466 883-6 PubMed GONUTS page
↑ Mount, DW et al. (1972) Dominant mutations (lex) in Escherichia coli K-12 which affect radiation sensitivity and frequency of ultraviolet lght-induced mutations. J. Bacteriol. 112 886-93 PubMed GONUTS page
↑ Lin, LL & Little, JW (1988) Isolation and characterization of noncleavable (Ind-) mutants of the LexA repressor of Escherichia coli K-12. J. Bacteriol. 170 2163-73 PubMed GONUTS page
↑ McCall, JO et al. (1987) Constitutive expression of the SOS response in recA718 mutants of Escherichia coli requires amplification of RecA718 protein. J. Bacteriol. 169 728-34 PubMed GONUTS page
↑ Little, JW & Harper, JE (1979) Identification of the lexA gene product of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 76 6147-51 PubMed GONUTS page
↑ Brent, R & Ptashne, M (1981) Mechanism of action of the lexA gene product. Proc. Natl. Acad. Sci. U.S.A. 78 4204-8 PubMed GONUTS page
↑ Little, JW et al. (1981) Purified lexA protein is a repressor of the recA and lexA genes. Proc. Natl. Acad. Sci. U.S.A. 78 4199-203 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:368030-1] Pacelli, LZ et al. (1979) Isolation and characterization of amber mutations in the lexA gene of Escherichia coli K-12. J. Bacteriol. 137 568-73 PubMed GONUTS page

[PMID:10760155-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 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:21912525-3] 3.0 ^3.1 Adikesavan, AK et al. (2011) Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites. PLoS Genet. 7 e1002244 PubMed GONUTS page

[PMID:21529368-4] 4.0 ^4.1 ^4.2 ^4.3 Cambray, G et al. (2011) Prevalence of SOS-mediated control of integron integrase expression as an adaptive trait of chromosomal and mobile integrons. Mob DNA 2 6 PubMed GONUTS page

[PMID:19210620-5] 5.0 ^5.1 ^5.2 ^5.3 Prysak, MH et al. (2009) Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage. Mol. Microbiol. 71 1071-87 PubMed GONUTS page

[PMID:24561554-6] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:20703307-7] Zhang, AP et al. (2010) Structure of the LexA-DNA complex and implications for SOS box measurement. Nature 466 883-6 PubMed GONUTS page

[PMID:4343824-8] Mount, DW et al. (1972) Dominant mutations (lex) in Escherichia coli K-12 which affect radiation sensitivity and frequency of ultraviolet lght-induced mutations. J. Bacteriol. 112 886-93 PubMed GONUTS page

[PMID:2834329-9] Lin, LL & Little, JW (1988) Isolation and characterization of noncleavable (Ind-) mutants of the LexA repressor of Escherichia coli K-12. J. Bacteriol. 170 2163-73 PubMed GONUTS page

[PMID:3542969-10] McCall, JO et al. (1987) Constitutive expression of the SOS response in recA718 mutants of Escherichia coli requires amplification of RecA718 protein. J. Bacteriol. 169 728-34 PubMed GONUTS page

[PMID:160562-11] Little, JW & Harper, JE (1979) Identification of the lexA gene product of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 76 6147-51 PubMed GONUTS page

[PMID:7027256-12] Brent, R & Ptashne, M (1981) Mechanism of action of the lexA gene product. Proc. Natl. Acad. Sci. U.S.A. 78 4204-8 PubMed GONUTS page

[PMID:7027255-13] Little, JW et al. (1981) Purified lexA protein is a repressor of the recA and lexA genes. Proc. Natl. Acad. Sci. U.S.A. 78 4199-203 PubMed GONUTS page

[PMID:18304323-14] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-15] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:LEXA

Contents

Annotations

Notes

References

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