Reviewed,
UniProtKB/Swiss-Prot Q65J42 (LEXA_BACLD)
Last modified
November 3, 2009.
Version 34.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: LexA repressor EC=3.4.21.88 | ||||
| Gene names |
| ||||
| Organism | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279010 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 207 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair DNA replication SOS response Transcription Transcription regulation |
| Ligand | DNA-binding |
| Molecular function | Hydrolase Repressor |
| PTM | Autocatalytic cleavage |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: HAMAP DNA replicationInferred from electronic annotation. Source: HAMAP SOS responseInferred from electronic annotation. Source: HAMAP negative regulation of transcription, DNA-dependentInferred from electronic annotation. Source: HAMAP proteolysisInferred from electronic annotation. Source: InterPro transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | DNA binding Inferred from electronic annotation. Source: HAMAP serine-type endopeptidase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 207 | 207 | LexA repressor HAMAP MF_00015 | PRO_0000170008 | |||||
Regions | |||||||||
| DNA binding | 28 – 48 | 21 | H-T-H motif By similarity | ||||||
Sites | |||||||||
| Active site | 129 | 1 | For autocatalytic cleavage activity By similarity | ||||||
| Active site | 167 | 1 | For autocatalytic cleavage activity By similarity | ||||||
| Site | 93 – 94 | 2 | Cleavage; by autolysis By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE017333 Genomic DNA. Translation: AAU40922.1. CP000002 Genomic DNA. Translation: AAU23560.1. | |
| RefSeq | YP_079198.1. YP_091615.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65J42. |
Genome annotation databases | |
| GeneID | 3031281. 3100705. |
| GenomeReviews | Gene locus BLi02032 in contig AE017333_GR. Gene locus BL00127 in contig CP000002_GR. |
| KEGG | bld:BLi02032. bli:BL00127. |
| NMPDR | fig|279010.5.peg.2730. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q65J42. |
| OMA | KVIGVFR. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010:BL00127-MON. |
Family and domain databases | |
| HAMAP | MF_00015. [Tree] |
| InterPro | IPR006199. 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] |
| Gene3D | G3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. |
| Pfam | PF01726. LexA_DNA_bind. 1 hit. PF00717. Peptidase_S24. 1 hit. [Graphical view] |
| PRINTS | PR00726. LEXASERPTASE. |
| TIGRFAMs | TIGR00498. lexA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LEXA_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65J42 Secondary accession number(s): Q62UJ9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

Clusters with


