Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

LexA repressor

Gene

lexA

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei126For autocatalytic cleavage activityUniRule annotation1
Active sitei164For autocatalytic cleavage activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi27 – 47H-T-H motifUniRule annotationAdd BLAST21

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

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
Ordered Locus Names:lmo1302
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
Proteomesi
  • UP000000817 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700531 – 204LexA repressorAdd BLAST204

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei90 – 91Cleavage; by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiQ8Y7H7.

Expressioni

Gene expression databases

CollecTFiEXPREG_000013e0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi169963.lmo1302.

Structurei

3D structure databases

ProteinModelPortaliQ8Y7H7.
SMRiQ8Y7H7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
KOiK01356.
OMAiKQHELLM.
PhylomeDBiQ8Y7H7.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
InterProiView protein in InterPro
IPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR006197. Peptidase_S24_LexA.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
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.

Q8Y7H7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKISKRQQDI YEFIKSEVKE KGYPPSVREI GEAVGLASSS TVHGHLARLE
60 70 80 90 100
GKGLIRRDPT KPRAIEILSL EDEAETPNVV NIPIIGKVTA GMPITAIENI
110 120 130 140 150
DEYFPLPEYM AAGETNVFML EIDGESMINA GILDGDKVIV RQESSAINGE
160 170 180 190 200
IVVAMTDENE ATCKRFYKEA NHFRLQPEND ALEPILLNNV TILGKVIGLY

RDIR
Length:204
Mass (Da):22,638
Last modified:March 1, 2002 - v1
Checksum:i05DBADBEC089F313
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591978 Genomic DNA. Translation: CAC99380.1.
PIRiAF1237.
RefSeqiNP_464827.1. NC_003210.1.
WP_009930693.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAC99380; CAC99380; CAC99380.
GeneIDi985139.
KEGGilmo:lmo1302.
PATRICi20311723. VBILisMon69206_1338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591978 Genomic DNA. Translation: CAC99380.1.
PIRiAF1237.
RefSeqiNP_464827.1. NC_003210.1.
WP_009930693.1. NC_003210.1.

3D structure databases

ProteinModelPortaliQ8Y7H7.
SMRiQ8Y7H7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo1302.

Protein family/group databases

MEROPSiS24.001.

Proteomic databases

PaxDbiQ8Y7H7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC99380; CAC99380; CAC99380.
GeneIDi985139.
KEGGilmo:lmo1302.
PATRICi20311723. VBILisMon69206_1338.

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
KOiK01356.
OMAiKQHELLM.
PhylomeDBiQ8Y7H7.

Gene expression databases

CollecTFiEXPREG_000013e0.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
InterProiView protein in InterPro
IPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR006197. Peptidase_S24_LexA.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiLEXA_LISMO
AccessioniPrimary (citable) accession number: Q8Y7H7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: March 1, 2002
Last modified: May 10, 2017
This is version 100 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.