Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A3MJD2 (LEXA_BURM7)

Last modified February 9, 2010. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    LexA repressor
    EC=3.4.21.88
Gene names
Name: lexA
Ordered Locus Names: BMA10247_0805
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length215 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 MF_00015

Catalytic activity

Hydrolysis of Ala-|-Gly bond in repressor lexA. HAMAP MF_00015

Subunit structure

Homodimer By similarity. HAMAP MF_00015

Sequence similarities

Belongs to the peptidase S24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215LexA repressor HAMAP MF_00015
PRO_1000001268

Regions

DNA binding28 – 4821H-T-H motif By similarity

Sites

Active site1331For autocatalytic cleavage activity By similarity
Active site1701For autocatalytic cleavage activity By similarity
Site98 – 992Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MJD2-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 713C9B66594842E5

FASTA21523,199
        10         20         30         40         50         60 
MIKLTARQQQ VFDLIRRAIE RSGFPPTRAE IAAELGFSSP NAAEEHLRAL ARKGVIELAA 

        70         80         90        100        110        120 
GASRGIRLLG IDDAPHQLTL PHAALMQLSL PLVGRVAAGS PILAQEHISQ HYACDPALFS 

       130        140        150        160        170        180 
SKPDYLLKVR GLSMRDAGIL DGDLLAVQKR TEAKDGQIIV ARLGDDVTVK RLKRRPGGVE 

       190        200        210 
LIAENPDYEN IFVKAGSAEF ALEGIAVGLI RPGEF 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000548 Genomic DNA. Translation: ABO04489.1.
RefSeqYP_001080368.1.

3D structure databases

SMRA3MJD2. Positions 1-69, 13-211, 90-215.
ModBaseSearch...

Genome annotation databases

GeneID4891690.
GenomeReviewsGene locus BMA10247_0805 in contig CP000548_GR.
KEGGbmn:BMA10247_0805.
TIGRBMA10247_0805.

Phylogenomic databases

HOGENOMHBG679610.
OMAKVIGVFR.

Family and domain databases

HAMAPMF_00015. LexA.
[Tree]
InterProIPR006199. LexA_DNA-bd_dom.
IPR006200. Pept_S24_LexA.
IPR006197. Peptidase_S24_LexA_cons-reg.
IPR019759. Peptidase_S24_S26_cons-reg.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00726. LEXASERPTASE.
TIGRFAMsTIGR00498. lexA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLEXA_BURM7
AccessionPrimary (citable) accession number: A3MJD2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: February 9, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents