UniProtKB - A7Z552 (LEXA_BACVZ)
Protein
LexA repressor
Gene
lexA
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum)
Status
Functioni
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.UniRule annotation
Catalytic activityi
- Hydrolysis of Ala-|-Gly bond in repressor LexA.UniRule annotation EC:3.4.21.88
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Active sitei | 128 | For autocatalytic cleavage activityUniRule annotation | 1 | |
| Active sitei | 166 | For autocatalytic cleavage activityUniRule annotation | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| DNA bindingi | 28 – 48 | H-T-H motifUniRule annotationAdd BLAST | 21 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-UniRule
- serine-type endopeptidase activity Source: UniProtKB-UniRule
GO - Biological processi
- DNA repair Source: UniProtKB-UniRule
- DNA replication Source: UniProtKB-UniRule
- negative regulation of transcription, DNA-templated Source: UniProtKB-UniRule
- SOS response Source: UniProtKB-UniRule
Keywordsi
| Molecular function | DNA-binding, Hydrolase, Repressor |
| Biological process | DNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation |
Enzyme and pathway databases
| BioCyci | BAMY326423:G1G84-1801-MONOMER |
Protein family/group databases
| MEROPSi | S24.001 |
Names & Taxonomyi
| Protein namesi | |
| Gene namesi | Name:lexAUniRule annotation Ordered Locus Names:RBAM_017650 |
| Organismi | Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum) |
| Taxonomic identifieri | 326423 [NCBI] |
| Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus amyloliquefaciens group › |
| Proteomesi |
|
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_1000001258 | 1 – 206 | LexA repressorAdd BLAST | 206 |
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 92 – 93 | Cleavage; by autolysisUniRule annotation | 2 |
Keywords - PTMi
Autocatalytic cleavageInteractioni
Subunit structurei
Homodimer.
UniRule annotationFamily & Domainsi
Sequence similaritiesi
Belongs to the peptidase S24 family.UniRule annotation
Phylogenomic databases
| HOGENOMi | CLU_066192_45_1_9 |
| OMAi | HVWLLPH |
Family and domain databases
| CDDi | cd00090, HTH_ARSR, 1 hit cd06529, S24_LexA-like, 1 hit |
| Gene3Di | 1.10.10.10, 1 hit |
| HAMAPi | MF_00015, LexA, 1 hit |
| InterProi | View protein in InterPro IPR011991, ArsR-like_HTH IPR006200, LexA IPR039418, LexA-like IPR036286, LexA/Signal_pep-like_sf IPR006199, LexA_DNA-bd_dom IPR006197, Peptidase_S24_LexA IPR015927, Peptidase_S24_S26A/B/C IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
| Pfami | View protein in Pfam PF01726, LexA_DNA_bind, 1 hit PF00717, Peptidase_S24, 1 hit |
| PRINTSi | PR00726, LEXASERPTASE |
| SUPFAMi | SSF46785, SSF46785, 1 hit SSF51306, SSF51306, 1 hit |
| TIGRFAMsi | TIGR00498, lexA, 1 hit |
Sequencei
Sequence statusi: Complete.
A7Z552-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTKLSKRQLD ILRFIKEEVK TKGYPPSVRE IGEAVGLASS STVHGHLARL
60 70 80 90 100
ETKGLIRRDP TKPRAIEVLD EEEVQIPKSQ VVNVPVIGKV TAGIPITAVE
110 120 130 140 150
NIDEYFPLPD RMVPPGEHVF MLEIMGESMI DAGIFDKDYV IVKQQNTANN
160 170 180 190 200
GEIVVAMTED DEATVKRFYK EDNYVRLQPE NPTMEPIILQ NVSILGKVIG
VFRTVH
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000560 Genomic DNA Translation: ABS74128.1 |
| RefSeqi | WP_012117646.1, NC_009725.2 |
Genome annotation databases
| EnsemblBacteriai | ABS74128; ABS74128; RBAM_017650 |
| KEGGi | bay:RBAM_017650 |
Similar proteinsi
Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000560 Genomic DNA Translation: ABS74128.1 |
| RefSeqi | WP_012117646.1, NC_009725.2 |
3D structure databases
| SMRi | A7Z552 |
| ModBasei | Search... |
Protein family/group databases
| MEROPSi | S24.001 |
Genome annotation databases
| EnsemblBacteriai | ABS74128; ABS74128; RBAM_017650 |
| KEGGi | bay:RBAM_017650 |
Phylogenomic databases
| HOGENOMi | CLU_066192_45_1_9 |
| OMAi | HVWLLPH |
Enzyme and pathway databases
| BioCyci | BAMY326423:G1G84-1801-MONOMER |
Family and domain databases
| CDDi | cd00090, HTH_ARSR, 1 hit cd06529, S24_LexA-like, 1 hit |
| Gene3Di | 1.10.10.10, 1 hit |
| HAMAPi | MF_00015, LexA, 1 hit |
| InterProi | View protein in InterPro IPR011991, ArsR-like_HTH IPR006200, LexA IPR039418, LexA-like IPR036286, LexA/Signal_pep-like_sf IPR006199, LexA_DNA-bd_dom IPR006197, Peptidase_S24_LexA IPR015927, Peptidase_S24_S26A/B/C IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
| Pfami | View protein in Pfam PF01726, LexA_DNA_bind, 1 hit PF00717, Peptidase_S24, 1 hit |
| PRINTSi | PR00726, LEXASERPTASE |
| SUPFAMi | SSF46785, SSF46785, 1 hit SSF51306, SSF51306, 1 hit |
| TIGRFAMsi | TIGR00498, lexA, 1 hit |
| ProtoNeti | Search... |
| MobiDBi | Search... |
Entry informationi
| Entry namei | LEXA_BACVZ | |
| Accessioni | A7Z552Primary (citable) accession number: A7Z552 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 15, 2008 |
| Last sequence update: | October 23, 2007 | |
| Last modified: | December 2, 2020 | |
| This is version 97 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
Miscellaneousi
Documents
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families




