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Reviewed, UniProtKB/Swiss-Prot A3N1B4 (LEXA_ACTP2)

Last modified February 9, 2010. Version 26. 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: APL_1108
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length210 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 – 210210LexA repressor HAMAP MF_00015
PRO_1000001252

Regions

DNA binding30 – 5021H-T-H motif By similarity

Sites

Active site1271For autocatalytic cleavage activity By similarity
Active site1641For autocatalytic cleavage activity By similarity
Site92 – 932Cleavage; by autolysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A3N1B4-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: C7C53005A658006E

FASTA21023,369
        10         20         30         40         50         60 
MSRKHLTARQ QEIFDFVKHH IETTGMPPTR VEIAREIGFK SPNAAEEHLK ALARKGYIEM 

        70         80         90        100        110        120 
LSGTSRGIRI LVDNEETAAN DDGLPLIGKV AAGTPIMAIE HVESHYPVNG AMFNPNADYL 

       130        140        150        160        170        180 
LKVNGNSMEK IGILDGDLLA VHKTNFARNG QVVVARVDDE VTVKRLEKKG DLIYLHPEND 

       190        200        210 
ELQPIIVDPR IEYIEIEGIA VGVIRNNAWM 

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000569 Genomic DNA. Translation: ABN74200.1.
RefSeqYP_001053805.1.

3D structure databases

SMRA3N1B4. Positions 4-206.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3N1B4.

Protein family/group databases

MEROPSS24.001.

Genome annotation databases

GeneID4849212.
GenomeReviewsGene locus APL_1108 in contig CP000569_GR.
KEGGapl:APL_1108.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1974.
HOGENOMHBG679610.
OMAKVIGVFR.
PhylomeDBA3N1B4.

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_ACTP2
AccessionPrimary (citable) accession number: A3N1B4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: February 9, 2010
This is version 26 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