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Protein

LexA repressor

Gene

lexA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: -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 sitei123For autocatalytic cleavage activityUniRule annotation1
Active sitei160For autocatalytic cleavage activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi28 – 48H-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
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700701 – 202LexA repressorAdd BLAST202

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei88 – 89Cleavage; by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP0A154
SMRiP0A154
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7 Bacteria
COG1974 LUCA

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.

P0A154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKLTPRQAE ILAFIKRCLE DNGFPPTRAE IAQELGFKSP NAAEEHLKAL
60 70 80 90 100
ARKGAIEMTP GASRGIRIPG LEAKAEEAGL PIIGRVAAGA PILAEQHIEQ
110 120 130 140 150
SCNINPAFFH PQADYLLRVH GMSMKDVGIF DGDLLAVHTC REARNGQIVV
160 170 180 190 200
ARIGDEVTVK RFKREGSKVW LLAENPEFAP IEVDLKEQEL VIEGLSVGVI

RR
Length:202
Mass (Da):22,148
Last modified:March 1, 2005 - v1
Checksum:iEF43C178C97D0679
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73A → T in CAC17802 (PubMed:11371535).Curated1
Sequence conflicti78A → N in CAC17802 (PubMed:11371535).Curated1
Sequence conflicti107A → S in CAC17802 (PubMed:11371535).Curated1
Sequence conflicti112Q → H in CAC17802 (PubMed:11371535).Curated1
Sequence conflicti167S → T in CAC17802 (PubMed:11371535).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63017 Genomic DNA Translation: CAA44749.1
AJ293485 Genomic DNA Translation: CAC17802.1
PIRiS30164
RefSeqiWP_010953131.1, NZ_NBWA01000015.1

Similar proteinsi

Entry informationi

Entry nameiLEXA_PSEPU
AccessioniPrimary (citable) accession number: P0A154
Secondary accession number(s): P37453, Q9EUU0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: October 25, 2017
This is version 67 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

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