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Protein

LexA repressor 1

Gene

lexA1

Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Status
Reviewed-Annotation score: Annotation score: 4 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 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

Names & Taxonomyi

Protein namesi
Recommended name:
LexA repressor 1UniRule annotation (EC:3.4.21.88UniRule annotation)
Gene namesi
Name:lexA1UniRule annotation
Synonyms:lexA, lexA-1
Ordered Locus Names:PP_2143
OrganismiPseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000556 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  • protein-DNA complex Source: CollecTF

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700691 – 202LexA repressor 1Add BLAST202

Sites

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

Keywords - PTMi

Autocatalytic cleavage

Expressioni

Gene expression databases

CollecTFiEXPREG_00000710.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi160488.PP_2143.

Structurei

3D structure databases

ProteinModelPortaliP0A153.
SMRiP0A153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232167.
KOiK01356.
OMAiRQMMQAM.

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.

P0A153-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN67756.1.
RefSeqiNP_744292.1. NC_002947.4.
WP_010953131.1. NC_002947.4.

Genome annotation databases

EnsemblBacteriaiAAN67756; AAN67756; PP_2143.
GeneIDi1044998.
KEGGippu:PP_2143.
PATRICifig|160488.4.peg.2260.

Similar proteinsi

Entry informationi

Entry nameiLEXA1_PSEPK
AccessioniPrimary (citable) accession number: P0A153
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 84 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