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Protein

LexA repressor

Gene

lexA

Organism
Lysinibacillus sphaericus (strain C3-41)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei127 – 1271For autocatalytic cleavage activityUniRule annotation
Active sitei165 – 1651For autocatalytic cleavage activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi28 – 4821H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Repressor

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciLSPH444177:GJEL-1724-MONOMER.

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:Bsph_1684
OrganismiLysinibacillus sphaericus (strain C3-41)
Taxonomic identifieri444177 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus
Proteomesi
  • UP000002164 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205LexA repressorPRO_1000089577Add
BLAST

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei91 – 922Cleavage; by autolysisUniRule annotation

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi444177.Bsph_1684.

Structurei

3D structure databases

ProteinModelPortaliB1HRJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
KOiK01356.
OMAiGVNDHLK.
OrthoDBiEOG6JHRHJ.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA.
InterProiIPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR00498. lexA. 1 hit.

Sequencei

Sequence statusi: Complete.

B1HRJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVSKRQED ILAFIKDEVR AKGYPPSVRE IGEAVGLASS STVHGHLARL
60 70 80 90 100
EQKGFIRRDP TKPRAIEILE PEESIQKQHV IHVPLVGKVT AGSPITAIEN
110 120 130 140 150
IEEYFPLPDT YGTSEDQLFM LEIMGESMIE AGILDGDLVI VKQKSTANNG
160 170 180 190 200
DIVVAMTAED EATVKRFFKE KNHFRLQPEN SSMEPIIVDQ VSIGGQVVGL

YRRVH
Length:205
Mass (Da):22,804
Last modified:April 29, 2008 - v1
Checksum:iE86217E32971FCEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000817 Genomic DNA. Translation: ACA39280.1.

Genome annotation databases

EnsemblBacteriaiACA39280; ACA39280; Bsph_1684.
KEGGilsp:Bsph_1684.
PATRICi22415867. VBILysSph89750_1800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000817 Genomic DNA. Translation: ACA39280.1.

3D structure databases

ProteinModelPortaliB1HRJ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi444177.Bsph_1684.

Protein family/group databases

MEROPSiS24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA39280; ACA39280; Bsph_1684.
KEGGilsp:Bsph_1684.
PATRICi22415867. VBILysSph89750_1800.

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
KOiK01356.
OMAiGVNDHLK.
OrthoDBiEOG6JHRHJ.

Enzyme and pathway databases

BioCyciLSPH444177:GJEL-1724-MONOMER.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA.
InterProiIPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR00498. lexA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species."
    Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., Berry C., Yuan Z.
    J. Bacteriol. 190:2892-2902(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C3-41.

Entry informationi

Entry nameiLEXA_LYSSC
AccessioniPrimary (citable) accession number: B1HRJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: June 8, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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.