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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. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847).The SOS response controls an apoptotic-like death (ALD) induced (in the absence of the mazE-mazF toxin-antitoxin module) in response to DNA damaging agents that is mediated by RecA and LexA (PubMed:22412352).UniRule annotation4 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei119For autocatalytic cleavage activityUniRule annotation1
Active sitei156For autocatalytic cleavage activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi28 – 48H-T-H motifUniRule annotationAdd BLAST21

GO - Molecular functioni

  • bacterial-type RNA polymerase transcriptional repressor activity, sequence-specific DNA binding Source: CollecTF
  • DNA binding Source: EcoliWiki
  • identical protein binding Source: IntAct
  • sequence-specific DNA binding Source: CollecTF
  • serine-type endopeptidase activity Source: InterPro
  • transcription regulatory region sequence-specific DNA binding Source: CollecTF

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • DNA repair Source: UniProtKB-KW
  • DNA replication Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: EcoliWiki
  • SOS response Source: EcoCyc
  • transcription, DNA-templated Source: EcoCyc

Keywordsi

Molecular functionDNA-binding, Hydrolase, Repressor
Biological processDNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:PD00205.
BRENDAi3.4.21.88. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10533. lexA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • protein-DNA complex Source: CollecTF

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700311 – 202LexA repressorAdd BLAST202

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84 – 85Cleavage; by autolysis2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiP0A7C2.
PRIDEiP0A7C2.

Expressioni

Gene expression databases

CollecTFiEXPREG_000007a0.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261718. 9 interactors.
DIPiDIP-51082N.
IntActiP0A7C2. 11 interactors.
MINTiMINT-1314348.
STRINGi316385.ECDH10B_4232.

Structurei

Secondary structure

1202
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 22Combined sources17
Helixi28 – 34Combined sources7
Helixi40 – 52Combined sources13
Beta strandi55 – 58Combined sources4
Beta strandi60 – 64Combined sources5
Beta strandi66 – 68Combined sources3
Beta strandi74 – 79Combined sources6
Helixi91 – 93Combined sources3
Beta strandi94 – 98Combined sources5
Helixi102 – 104Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi111 – 114Combined sources4
Helixi121 – 123Combined sources3
Beta strandi130 – 135Combined sources6
Beta strandi143 – 149Combined sources7
Beta strandi152 – 161Combined sources10
Beta strandi164 – 168Combined sources5
Beta strandi172 – 174Combined sources3
Beta strandi177 – 180Combined sources4
Turni181 – 183Combined sources3
Beta strandi186 – 197Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7C2.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232167.
InParanoidiP0A7C2.
KOiK01356.
PhylomeDBiP0A7C2.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
InterProiView protein in InterPro
IPR006200. LexA.
IPR036286. LexA/Signal_pep-like_sf.
IPR006199. LexA_DNA-bd_dom.
IPR006197. Peptidase_S24_LexA.
IPR015927. Peptidase_S24_S26A/B/C.
IPR036388. WH-like_DNA-bd_sf.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51306. 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)DescriptionActionsGraphical viewLength
Natural varianti85G → D in lexA3, resistant to cleavage. Increased sensitivity to hydroxyurea. 2 Publications1

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.
WP_000646078.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77013; AAC77013; b4043.
BAE78045; BAE78045; BAE78045.
GeneIDi948544.
KEGGiecj:JW4003.
eco:b4043.
PATRICifig|511145.12.peg.4160.

Similar proteinsi

Entry informationi

Entry nameiLEXA_ECOLI
AccessioniPrimary (citable) accession number: P0A7C2
Secondary accession number(s): P03033, Q2M6R1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 25, 2017
This is version 114 of the entry and version 1 of the sequence. See 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