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E4TG52 (E4TG52_CALNY) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00015 SAAS SAAS019759

Catalytic activity

Hydrolysis of Ala-|-Gly bond in repressor LexA. HAMAP-Rule MF_00015 SAAS SAAS019759

Subunit structure

Homodimer By similarity. SAAS SAAS019759 HAMAP-Rule MF_00015

Sequence similarities

Belongs to the peptidase S24 family. RuleBase RU003991 HAMAP-Rule MF_00015

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

DNA binding27 – 4721H-T-H motif By similarity HAMAP-Rule MF_00015

Sites

Active site1171For autocatalytic cleavage activity By similarity HAMAP-Rule MF_00015
Active site1541For autocatalytic cleavage activity By similarity HAMAP-Rule MF_00015
Site82 – 832Cleavage; by autolysis By similarity HAMAP-Rule MF_00015

Sequences

Sequence LengthMass (Da)Tools
E4TG52 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: A54DD314E769234C

FASTA20623,394
        10         20         30         40         50         60 
MDLTDRQKEC INFISRFIKD YGYPPTIQEI CNNLGIRSKN AGFKLLNALE SKGFIRRNRS 

        70         80         90        100        110        120 
ISRGIELLKI NNGIPILGRI TAGIPIDAEE NIEGYIPLED ILGDISGYFG LRVIGDSMVE 

       130        140        150        160        170        180 
KGILDGDIAI IKKQPDILNN QVGAFMINGE FTLKTFKMMD DGRIYLKPEN NKYKPIYITE 

       190        200 
NDTFEVVGLL KMVVRLFGED YEARKY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002347 Genomic DNA. Translation: ADR18602.1.
RefSeqYP_004050765.1. NC_014758.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS24.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADR18602; ADR18602; Calni_0691.
GeneID10008702.
KEGGcni:Calni_0691.
PATRIC45189099. VBICalNit163602_0764.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000232167.
KOK01356.
OMAWLEPANS.

Enzyme and pathway databases

BioCycCNIT768670:GHD1-704-MONOMER.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPMF_00015. LexA.
InterProIPR006200. 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]
PfamPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00726. LEXASERPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
TIGRFAMsTIGR00498. lexA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameE4TG52_CALNY
AccessionPrimary (citable) accession number: E4TG52
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: June 11, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)