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Reviewed, UniProtKB/Swiss-Prot A7GR32 (LEXA_BACCN)

Last modified November 3, 2009. Version 18. 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: Bcer98_2344
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the peptidase S24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206LexA repressor HAMAP MF_00015
PRO_1000074047

Regions

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

Sites

Active site1281For autocatalytic cleavage activity By similarity
Active site1661For autocatalytic cleavage activity By similarity
Site92 – 932Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GR32-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C63A6401E23FCB21

FASTA20622,789
        10         20         30         40         50         60 
MEKLTKRQQD ILDFIKLKVQ EKGYPPSVRE IGQAVGLASS STVHGHLSRL EEKGYIRRDP 

        70         80         90        100        110        120 
TKPRAIEILG EERIEISTQS VVQVPIVGKV TAGLPITAVE SVEEHFPLPA SIIAGADQVF 

       130        140        150        160        170        180 
MLRISGDSMI EAGIFDGDLV VVRQQHSANN GEIVVALTED NEATVKRFYK EKDHFRLQPE 

       190        200 
NSSLEPIILN TVSVIGKVIG VYRDLH 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000764 Genomic DNA. Translation: ABS22590.1.
RefSeqYP_001375585.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7GR32.

Protein family/group databases

MEROPSS24.001.

Genome annotation databases

GeneID5343758.
GenomeReviewsGene locus Bcer98_2344 in contig CP000764_GR.
KEGGbcy:Bcer98_2344.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAKVIGVFR.

Family and domain databases

HAMAPMF_00015.
[Tree]
InterProIPR006199. LexA_DNA_bd.
IPR006200. Pept_S24_LexA.
IPR006197. Peptidase_S24_LexA_cons-reg.
IPR019759. Peptidase_S24_S26_cons-reg.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR011991. Wing_hlx_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_BACCN
AccessionPrimary (citable) accession number: A7GR32
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 18 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