Reviewed,
UniProtKB/Swiss-Prot Q6FZU5 (LEXA_BARQU)
Last modified
February 9, 2010.
Version 37.
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 | Bartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 803 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 237 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: 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 – 237 | 237 | LexA repressor HAMAP MF_00015 | PRO_0000170012 | |||||
Regions | |||||||||
| DNA binding | 26 – 46 | 21 | H-T-H motif By similarity | ||||||
Sites | |||||||||
| Active site | 158 | 1 | For autocatalytic cleavage activity By similarity | ||||||
| Active site | 196 | 1 | For autocatalytic cleavage activity By similarity | ||||||
| Site | 123 – 124 | 2 | Cleavage; by autolysis By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX897700 Genomic DNA. Translation: CAF26107.1. |
| RefSeq | YP_032265.1. |
3D structure databases | |
| SMR | Q6FZU5. Positions 115-237. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S24.001. |
Genome annotation databases | |
| GeneID | 2866428. |
| GenomeReviews | Gene locus BQ06160 in contig BX897700_GR. |
| KEGG | bqu:BQ06160. |
| NMPDR | fig|283165.1.peg.535. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG679610. |
| OMA | AILTFIR. |
Enzyme and pathway databases | |
| BioCyc | BQUI283165:BQ06160-MONOMER. |
| BRENDA | 3.4.21.88. 292235. |
Family and domain databases | |
| HAMAP | MF_00015. LexA. [Tree] |
| InterPro | IPR006199. 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] |
| 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_BARQU | ||||||||
| Accession | Primary (citable) accession number: Q6FZU5 | ||||||||
| 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


