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P0A7C2 (LEXA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LexA repressor

EC=3.4.21.88
Gene names
Name:lexA
Synonyms:exrA, spr, tsl, umuA
Ordered Locus Names:b4043, JW4003
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rpsEP0A7W11EBI-553416,EBI-543949

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202LexA repressor HAMAP-Rule MF_00015
PRO_0000170031

Regions

DNA binding28 – 4821H-T-H motif HAMAP-Rule MF_00015

Sites

Active site1191For autocatalytic cleavage activity By similarity
Active site1561For autocatalytic cleavage activity By similarity
Site84 – 852Cleavage; by autolysis

Natural variations

Natural variant851G → D in lexA3, resistant to cleavage.

Secondary structure

........................................ 202
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7C2 [UniParc].

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

FASTA20222,358
        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' 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 277:1453-1462(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.
PIRILEC. A90808.
RefSeqNP_418467.1. NC_000913.3.
YP_492186.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JHCX-ray2.00A68-202[»]
1JHEX-ray2.50A/B68-202[»]
1JHFX-ray1.80A/B1-202[»]
1JHHX-ray2.10A/B1-202[»]
1LEANMR-A1-84[»]
1LEBNMR-A1-84[»]
1MVDmodel-A/B1-202[»]
1QAAmodel-A/B1-202[»]
3JSOX-ray2.29A/B1-202[»]
3JSPX-ray2.90A/B1-202[»]
3K3RX-ray3.20E/F1-202[»]
ProteinModelPortalP0A7C2.
SMRP0A7C2. Positions 1-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-51082N.
IntActP0A7C2. 11 interactions.
MINTMINT-1314348.
STRING511145.b4043.

Protein family/group databases

MEROPSS24.001.

Proteomic databases

PaxDbP0A7C2.
PRIDEP0A7C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77013; AAC77013; b4043.
BAE78045; BAE78045; BAE78045.
GeneID12932724.
948544.
KEGGecj:Y75_p3930.
eco:b4043.
PATRIC32123623. VBIEscCol129921_4160.

Organism-specific databases

EchoBASEEB0528.
EcoGeneEG10533. lexA.

Phylogenomic databases

eggNOGCOG1974.
HOGENOMHOG000232167.
KOK01356.
OMAQNTANNG.
OrthoDBEOG6JHRHJ.
PhylomeDBP0A7C2.
ProtClustDBPRK00215.

Enzyme and pathway databases

BioCycEcoCyc:PD00205.
ECOL316407:JW4003-MONOMER.

Gene expression databases

GenevestigatorP0A7C2.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPMF_00015. LexA.
InterProIPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00726. LEXASERPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
TIGRFAMsTIGR00498. lexA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A7C2.
PROP0A7C2.

Entry information

Entry nameLEXA_ECOLI
AccessionPrimary (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: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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