Q0VQU1 (LEXA_ALCBS) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: LexA repressor EC=3.4.21.88 | ||||
| Gene names |
| ||||
| Organism | Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 393595 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax |
Protein attributes
| Sequence length | 204 AA. |
| Sequence status | Complete. |
| 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. 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. |
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: UniProtKB-KW DNA replicationInferred from electronic annotation. Source: UniProtKB-KW SOS responseInferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 204 | 204 | LexA repressor HAMAP MF_00015 | PRO_1000001254 | |||||
Regions | |||||||||
| DNA binding | 29 – 49 | 21 | H-T-H motif By similarity | ||||||
Sites | |||||||||
| Active site | 123 | 1 | For autocatalytic cleavage activity By similarity | ||||||
| Active site | 160 | 1 | For autocatalytic cleavage activity By similarity | ||||||
| Site | 88 – 89 | 2 | Cleavage; by autolysis By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. Golyshin P.N.Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK2 / ATCC 700651 / DSM 11573. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM286690 Genomic DNA. Translation: CAL16457.1. |
| RefSeq | YP_692729.1. NC_008260.1. |
3D structure databases | |
| ProteinModelPortal | Q0VQU1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0VQU1. |
Protein family/group databases | |
| MEROPS | S24.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4211543. |
| GenomeReviews | Gene locus ABO_1009 in contig AM286690_GR. |
| KEGG | abo:ABO_1009. |
| NMPDR | fig|393595.12.peg.1016. |
| PATRIC | 20839741. VBIAlcBor124741_1061. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1974. |
| HOGENOM | HBG679610. |
| OMA | THRHSPS. |
| PhylomeDB | Q0VQU1. |
Enzyme and pathway databases | |
| BioCyc | ABOR393595:ABO_1009-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00015. LexA. [Tree] |
| InterPro | IPR006199. LexA_DNA-bd_dom. IPR006200. Pept_S24_LexA. IPR006197. Peptidase_S24_LexA. IPR019759. Peptidase_S24_S26. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. IPR011991. WHTH_trsnscrt_rep_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. |
| KO | K01356. |
| Pfam | PF01726. LexA_DNA_bind. 1 hit. PF00717. Peptidase_S24. 1 hit. [Graphical view] |
| PRINTS | PR00726. LEXASERPTASE. |
| SUPFAM | SSF51306. Pept_S24_S26_C. 1 hit. |
| TIGRFAMs | TIGR00498. LexA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LEXA_ALCBS | ||||||||
| Accession | Primary (citable) accession number: Q0VQU1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with