LexA repressor - Escherichia coli (strain K12)

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P0A7C2 (LEXA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
LexA repressor
EC=3.4.21.88

Gene names

Name:	lexA
Synonyms:	exrA, spr, tsl, umuA
Ordered Locus Names:	b4043, JW4003

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	202 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. Ref.9 Ref.10
Catalytic activity	Hydrolysis of Ala-\|-Gly bond in repressor lexA. HAMAP-Rule MF_00015
Subunit structure	Homodimer.
Sequence similarities	Belongs to the peptidase S24 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication SOS response Transcription Transcription regulation
Ligand	DNA-binding
Molecular function	Hydrolase Repressor
PTM	Autocatalytic cleavage
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: HAMAP DNA replication Inferred from electronic annotation. Source: HAMAP SOS response Inferred from mutant phenotype PubMed 3542969. Source: EcoCyc negative regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 10760155. Source: EcoliWiki proteolysis Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from mutant phenotype PubMed 2834329. Source: EcoliWiki transcription, DNA-dependent Inferred from direct assay Ref.9 Ref.10. Source: EcoCyc
Molecular_function	DNA binding Inferred from direct assay PubMed 10760155. Source: EcoliWiki serine-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rpsE	P0A7W1	1	EBI-553416,EBI-543949

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 202

202

LexA repressor HAMAP-Rule MF_00015

PRO_0000170031

Regions

DNA binding

28 – 48

H-T-H motif HAMAP-Rule MF_00015

Sites

Active site

119

For autocatalytic cleavage activity By similarity

Active site

156

For autocatalytic cleavage activity By similarity

Site

84 – 85

Cleavage; by autolysis

Natural variations

Natural variant

G → D in lexA3, resistant to cleavage.

Secondary structure

202

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7C2 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7E8816A32C19EE71
Show »

FASTA

202

22,358

        10         20         30         40         50         60 
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL ARKGVIEIVS 

        70         80         90        100        110        120 
GASRGIRLLQ EEEEGLPLVG RVAAGEPLLA QQHIEGHYQV DPSLFKPNAD FLLRVSGMSM 

       130        140        150        160        170        180 
KDIGIMDGDL LAVHKTQDVR NGQVVVARID DEVTVKRLKK QGNKVELLPE NSEFKPIVVD 

       190        200 
LRQQSFTIEG LAVGVIRNGD WL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the lexA gene of E. coli." Horii T., Ogawa T., Ogawa H. Cell 23:689-697(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the lexA gene of Escherichia coli K-12." Markham B.E., Little J.W., Mount D.W. Nucleic Acids Res. 9:4149-4161(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT LEXA3. Strain: K12.
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Genetic analysis of the LexA repressor: isolation and characterization of LexA(Def) mutant proteins." Oertel-Buchheit P., Lamerichs R.M., Schnarr M., Granger-Schnarr M. Mol. Gen. Genet. 223:40-48(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
[7]	"Organization of the lexA gene of Escherichia coli and nucleotide sequence of the regulatory region." Miki T., Ebina Y., Kishi F., Nakazawa A. Nucleic Acids Res. 9:529-543(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
[8]	Lilley P.E., Dixon N.E. Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-202. Strain: K12.
[9]	"Purified lexA protein is a repressor of the recA and lexA genes." Little J.W., Mount D.W., Yanisch-Perron C.R. Proc. Natl. Acad. Sci. U.S.A. 78:4199-4203(1981) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Mechanism of action of the lexA gene product." Brent R., Ptashne M. Proc. Natl. Acad. Sci. U.S.A. 78:4204-4208(1981) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study." Lamerichs R.M.J.N., Padilla A., Boelens R., Kaptein R., Ottleben G., Rueterjans H., Granger-Schnarr M., Oertel P., Schnarr M. Proc. Natl. Acad. Sci. U.S.A. 86:6863-6867(1989) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[12]	"Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy." Fogh R.H., Ottleben G., Rueterjans H., Schnarr M., Boelens R., Kaptein R. EMBO J. 13:3936-3944(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[13]	"A model for the LexA repressor DNA complex." Knegtel R.M.A., Fogh R.H., Ottleben G., Rueterjans H., Dumoulin P., Schnarr M., Boelens R., Kaptein R. Proteins 21:226-236(1995) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01643 Genomic DNA. Translation: AAA24067.1.
U00006 Genomic DNA. Translation: AAC43137.1.
U00096 Genomic DNA. Translation: AAC77013.1.
AP009048 Genomic DNA. Translation: BAE78045.1.
L02362 Genomic DNA. Translation: AAA24068.1.

PIR

ILEC. A90808.

RefSeq

NP_418467.1. NC_000913.2.
YP_492186.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JHC	X-ray	2.00	A	68-202	[»]
1JHE	X-ray	2.50	A/B	68-202	[»]
1JHF	X-ray	1.80	A/B	1-202	[»]
1JHH	X-ray	2.10	A/B	1-202	[»]
1LEA	NMR	-	A	1-84	[»]
1LEB	NMR	-	A	1-84	[»]
1MVD	model	-	A/B	1-202	[»]
1QAA	model	-	A/B	1-202	[»]
3JSO	X-ray	2.29	A/B	1-202	[»]
3JSP	X-ray	2.90	A/B	1-202	[»]
3K3R	X-ray	3.20	E/F	1-202	[»]

ProteinModelPortal

P0A7C2.

SMR

P0A7C2. Positions 1-199.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-51082N.

IntAct

P0A7C2. 3 interactions.

MINT

MINT-1314348.

STRING

511145.b4043.

Protein family/group databases

MEROPS

S24.001.

Proteomic databases

PaxDb

P0A7C2.

PRIDE

P0A7C2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77013; AAC77013; b4043.
BAE78045; BAE78045; BAE78045.

GeneID

12932724.
948544.

KEGG

ecj:Y75_p3930.
eco:b4043.

PATRIC

32123623. VBIEscCol129921_4160.

Organism-specific databases

EchoBASE

EB0528.

EcoGene

EG10533. lexA.

Phylogenomic databases

eggNOG

COG1974.

HOGENOM

HOG000232167.

K01356.

OMA

RGDSMKN.

ProtClustDB

PRK00215.

Enzyme and pathway databases

BioCyc

EcoCyc:PD00205.
ECOL316407:JW4003-MONOMER.

Gene expression databases

Genevestigator

P0A7C2.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
2.10.109.10. 1 hit.

HAMAP

MF_00015. LexA.

InterPro

IPR006199. LexA_DNA-bd_dom.
IPR006200. Pept_S24_LexA.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]

PRINTS

PR00726. LEXASERPTASE.

SUPFAM

SSF51306. Pept_S24_S26_C. 1 hit.

TIGRFAMs

TIGR00498. lexA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7C2.

Entry information

Entry name

LEXA_ECOLI

Accession

Primary (citable) accession number: P0A7C2
Secondary accession number(s): P03033, Q2M6R1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents