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Protein

LexA repressor

Gene

lexA

Organism
Thermotoga neapolitana
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 sitei119For autocatalytic cleavage activityUniRule annotation1
Active sitei156For autocatalytic cleavage activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi28 – 47H-T-H motifUniRule annotationAdd BLAST20

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
OrganismiThermotoga neapolitana
Taxonomic identifieri2337 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700991 – 197LexA repressorAdd BLAST197

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei83 – 84Cleavage; by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi309803.CTN_1487.

Structurei

3D structure databases

ProteinModelPortaliO86948.
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.
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.

O86948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDLTAKQRS VLIFIEEFIE KNGYPPSVRE IARRFRITPR GAQLHLVALE
60 70 80 90 100
KKGYIERKNG KPRAMRVTKS VKNRVPLIGE IRAGEKKEAI EYLEDYIEVP
110 120 130 140 150
GSFLSSGYEH FLLRVKGESM IEEHICDGDL VLIRRQDWAQ NGDIVAAMVE
160 170 180 190
GEVTLKKFFQ RGEMVELRPA NKEMSPMFFR ADRVKILGKV VGVFRKI
Length:197
Mass (Da):22,708
Last modified:November 1, 1998 - v1
Checksum:iCDE332CBA1C8A1B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007446 Genomic DNA. Translation: CAA07513.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007446 Genomic DNA. Translation: CAA07513.1.

3D structure databases

ProteinModelPortaliO86948.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309803.CTN_1487.

Protein family/group databases

MEROPSiS24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.

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_THENE
AccessioniPrimary (citable) accession number: O86948
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

No consensus sequence similar to the SOS-box from E.coli or from B.subtilis was found upstream of the lexA gene, suggesting the presence of another target sequence specific for the Thermotogales.

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.