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Protein

LexA repressor

Gene

lexA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 PublicationsUniRule annotation

Catalytic activityi

Hydrolysis of Ala-|-Gly bond in repressor LexA.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 852Cleavage; by autolysis
Active sitei119 – 1191For autocatalytic cleavage activityUniRule annotation
Active sitei156 – 1561For autocatalytic cleavage activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi28 – 4821H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: EcoliWiki
  2. serine-type endopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. DNA repair Source: UniProtKB-HAMAP
  3. DNA replication Source: UniProtKB-HAMAP
  4. negative regulation of transcription, DNA-templated Source: EcoliWiki
  5. SOS response Source: EcoCyc
  6. transcription, DNA-templated Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Repressor

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00205.
ECOL316407:JW4003-MONOMER.

Protein family/group databases

MEROPSiS24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
LexA repressorUniRule annotation (EC:3.4.21.88UniRule annotation)
Gene namesi
Name:lexAUniRule annotation
Synonyms:exrA, spr, tsl, umuA
Ordered Locus Names:b4043, JW4003
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10533. lexA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202LexA repressorPRO_0000170031Add
BLAST

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiP0A7C2.
PRIDEiP0A7C2.

Expressioni

Gene expression databases

GenevestigatoriP0A7C2.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsEP0A7W11EBI-553416,EBI-543949

Protein-protein interaction databases

DIPiDIP-51082N.
IntActiP0A7C2. 11 interactions.
MINTiMINT-1314348.
STRINGi511145.b4043.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2217Combined sources
Helixi28 – 347Combined sources
Helixi40 – 5213Combined sources
Beta strandi55 – 584Combined sources
Beta strandi60 – 645Combined sources
Beta strandi66 – 683Combined sources
Beta strandi74 – 796Combined sources
Helixi91 – 933Combined sources
Beta strandi94 – 985Combined sources
Helixi102 – 1043Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi111 – 1144Combined sources
Helixi121 – 1233Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi143 – 1497Combined sources
Beta strandi152 – 16110Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi177 – 1804Combined sources
Turni181 – 1833Combined sources
Beta strandi186 – 19712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A7C2.
SMRiP0A7C2. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7C2.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1974.
HOGENOMiHOG000232167.
InParanoidiP0A7C2.
KOiK01356.
OMAiIAETGMP.
OrthoDBiEOG6JHRHJ.
PhylomeDBiP0A7C2.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA.
InterProiIPR006200. 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]
PfamiPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR00498. lexA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A7C2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL
60 70 80 90 100
ARKGVIEIVS GASRGIRLLQ EEEEGLPLVG RVAAGEPLLA QQHIEGHYQV
110 120 130 140 150
DPSLFKPNAD FLLRVSGMSM KDIGIMDGDL LAVHKTQDVR NGQVVVARID
160 170 180 190 200
DEVTVKRLKK QGNKVELLPE NSEFKPIVVD LRQQSFTIEG LAVGVIRNGD

WL
Length:202
Mass (Da):22,358
Last modified:July 21, 1986 - v1
Checksum:i7E8816A32C19EE71
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851G → D in lexA3, resistant to cleavage.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA90808. ILEC.
RefSeqiNP_418467.1. NC_000913.3.
YP_492186.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77013; AAC77013; b4043.
BAE78045; BAE78045; BAE78045.
GeneIDi12932724.
948544.
KEGGiecj:Y75_p3930.
eco:b4043.
PATRICi32123623. VBIEscCol129921_4160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA90808. ILEC.
RefSeqiNP_418467.1. NC_000913.3.
YP_492186.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A7C2.
SMRiP0A7C2. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-51082N.
IntActiP0A7C2. 11 interactions.
MINTiMINT-1314348.
STRINGi511145.b4043.

Protein family/group databases

MEROPSiS24.001.

Proteomic databases

PaxDbiP0A7C2.
PRIDEiP0A7C2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77013; AAC77013; b4043.
BAE78045; BAE78045; BAE78045.
GeneIDi12932724.
948544.
KEGGiecj:Y75_p3930.
eco:b4043.
PATRICi32123623. VBIEscCol129921_4160.

Organism-specific databases

EchoBASEiEB0528.
EcoGeneiEG10533. lexA.

Phylogenomic databases

eggNOGiCOG1974.
HOGENOMiHOG000232167.
InParanoidiP0A7C2.
KOiK01356.
OMAiIAETGMP.
OrthoDBiEOG6JHRHJ.
PhylomeDBiP0A7C2.

Enzyme and pathway databases

BioCyciEcoCyc:PD00205.
ECOL316407:JW4003-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7C2.
PROiP0A7C2.

Gene expression databases

GenevestigatoriP0A7C2.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA.
InterProiIPR006200. 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]
PfamiPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR00498. lexA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiLEXA_ECOLI
AccessioniPrimary (citable) accession number: P0A7C2
Secondary accession number(s): P03033, Q2M6R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.