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Protein

LexA repressor

Gene

lexA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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
Ordered Locus Names:TM_1082
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001700981 – 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

STRINGi243274.TM1082.

Structurei

Secondary structure

1197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 22Combined sources17
Helixi28 – 35Combined sources8
Helixi39 – 51Combined sources13
Beta strandi54 – 56Combined sources3
Helixi58 – 60Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi74 – 83Combined sources10
Helixi85 – 87Combined sources3
Beta strandi89 – 98Combined sources10
Helixi101 – 103Combined sources3
Beta strandi110 – 114Combined sources5
Helixi121 – 123Combined sources3
Beta strandi130 – 135Combined sources6
Beta strandi144 – 149Combined sources6
Beta strandi152 – 161Combined sources10
Beta strandi164 – 168Combined sources5
Beta strandi177 – 180Combined sources4
Helixi181 – 183Combined sources3
Beta strandi185 – 196Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K2ZX-ray1.37A/B3-197[»]
ProteinModelPortaliO33927.
SMRiO33927.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33927.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
InParanoidiO33927.
KOiK01356.
OMAiKQHELLM.

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.

O33927-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDLTERQRK VLLFIEEFIE KNGYPPSVRE IARRFRITPR GALLHLIALE
60 70 80 90 100
KKGYIERKNG KPRALRISKS IRNKIPLIGE IRAGEKREAI EYLEDYIEIP
110 120 130 140 150
ESFLSSGYDH FLLKVKGESM IEEHICDGDL VLVRRQDWAQ NGDIVAAMVD
160 170 180 190
GEVTLKKFYQ RGDTVELRPA NREMSSMFFR AEKVKILGKV VGVFRKL
Length:197
Mass (Da):22,864
Last modified:January 1, 1998 - v1
Checksum:iA8093B0BB3D10BFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76417 Genomic DNA. Translation: AAB87145.1.
AE000512 Genomic DNA. Translation: AAD36159.1.
PIRiB72297.
RefSeqiNP_228888.1. NC_000853.1.
WP_004080401.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36159; AAD36159; TM_1082.
GeneIDi897745.
KEGGitma:TM1082.
PATRICi23937093. VBITheMar51294_1095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76417 Genomic DNA. Translation: AAB87145.1.
AE000512 Genomic DNA. Translation: AAD36159.1.
PIRiB72297.
RefSeqiNP_228888.1. NC_000853.1.
WP_004080401.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K2ZX-ray1.37A/B3-197[»]
ProteinModelPortaliO33927.
SMRiO33927.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1082.

Protein family/group databases

MEROPSiS24.001.

Protocols and materials databases

DNASUi897745.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36159; AAD36159; TM_1082.
GeneIDi897745.
KEGGitma:TM1082.
PATRICi23937093. VBITheMar51294_1095.

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
InParanoidiO33927.
KOiK01356.
OMAiKQHELLM.

Miscellaneous databases

EvolutionaryTraceiO33927.

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_THEMA
AccessioniPrimary (citable) accession number: O33927
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 128 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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.