A1A2G3 · LEXA_BIFAA

Function

function

Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. 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.

Catalytic activity

  • Hydrolysis of Ala-|-Gly bond in repressor LexA.
    EC:3.4.21.88 (UniProtKB | ENZYME | Rhea)

Features

Showing features for dna binding, site, active site.

125720406080100120140160180200220240
TypeIDPosition(s)Description
DNA binding64-84H-T-H motif
Site146-147Cleavage; by autolysis
Active site181For autocatalytic cleavage activity
Active site218For autocatalytic cleavage activity

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular FunctionDNA binding
Molecular Functionserine-type endopeptidase activity
Biological ProcessDNA repair
Biological ProcessDNA replication
Biological Processnegative regulation of DNA-templated transcription
Biological Processproteolysis
Biological ProcessSOS response

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    LexA repressor
  • EC number

Gene names

    • Name
      lexA
    • Ordered locus names
      BAD_1115

Organism names

Accessions

  • Primary accession
    A1A2G3

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003227151-257LexA repressor

Keywords

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase S24 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    28,169
  • Last updated
    2007-01-23 v1
  • Checksum
    413955312B4982DD
MFDFIGVSRYASKELRKEPIVSTIPFTPKKSDERPDESTLTDRQRKVLDAIKTHLAKQGFAPSFREIGEAAGLKSPSSVKHQLQVLDEKGFIRMNANKGRAIEVVNLNDEEPNGKVAQVIPFPSQDDACGSIMASHDVPLVGRIAAGVPITAEQHVDDVMRLPERLTGTGNLFMLEVHGDSMIDAAICDGDFVVVREQNSAENGDIVAALLDDEATVKTFRKDHGHVWLIPHNPAYSPIDGTHAEIMGKVVTVLRKI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009256
EMBL· GenBank· DDBJ
BAF39896.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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