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Protein

LexA repressor

Gene

lexA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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 sitei158For autocatalytic cleavage activityUniRule annotation1
Active sitei195For autocatalytic cleavage activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi52 – 72H-T-H motifUniRule annotationAdd BLAST21

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

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:SCO5803
ORF Names:SC4H2.24c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700961 – 234LexA repressorAdd BLAST234

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei123 – 124Cleavage; by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PRIDEiO69979.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO5803.

Structurei

3D structure databases

ProteinModelPortaliO69979.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
InParanoidiO69979.
KOiK01356.
OMAiKQHELLM.
OrthoDBiPOG091H029U.
PhylomeDBiO69979.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
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.

O69979-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAANPEGH KRSLPGRPPG IRADSSGLTD RQRRVIEVIR DSVQRRGYPP
60 70 80 90 100
SMREIGQAVG LSSTSSVAHQ LMALERKGFL RRDPHRPRAY EVRGSDQAAS
110 120 130 140 150
VQPTDTAGKP AASYVPLVGR IAAGGPILAE ESVEDVFPLP RQLVGDGELF
160 170 180 190 200
VLKVVGDSMI EAAICDGDWV TVRRQPVAEN GDIVAAMLDG EATVKRFKRE
210 220 230
DGHVWLLPHN SAYEPIPGDD ATILGKVVAV LRRV
Length:234
Mass (Da):25,311
Last modified:August 1, 1998 - v1
Checksum:i8AB5C3266B8F678A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939125 Genomic DNA. Translation: CAA18339.1.
PIRiT35123.
RefSeqiNP_629927.1. NC_003888.3.
WP_011030466.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAA18339; CAA18339; CAA18339.
GeneIDi1101245.
KEGGisco:SCO5803.
PATRICi23741496. VBIStrCoe124346_5895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939125 Genomic DNA. Translation: CAA18339.1.
PIRiT35123.
RefSeqiNP_629927.1. NC_003888.3.
WP_011030466.1. NC_003888.3.

3D structure databases

ProteinModelPortaliO69979.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5803.

Protein family/group databases

MEROPSiS24.001.

Proteomic databases

PRIDEiO69979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAA18339; CAA18339; CAA18339.
GeneIDi1101245.
KEGGisco:SCO5803.
PATRICi23741496. VBIStrCoe124346_5895.

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
InParanoidiO69979.
KOiK01356.
OMAiKQHELLM.
OrthoDBiPOG091H029U.
PhylomeDBiO69979.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
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...

Entry informationi

Entry nameiLEXA_STRCO
AccessioniPrimary (citable) accession number: O69979
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 116 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, 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.