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Protein

LexA repressor

Gene

lexA

Organism
Peptoclostridium difficile (strain 630) (Clostridium difficile)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311For autocatalytic cleavage activityUniRule annotation
Active sitei169 – 1691For autocatalytic cleavage activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi29 – 4921H-T-H motifUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Repressor

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, SOS response, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Protein family/group databases

MEROPSiS24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
LexA repressorUniRule annotation (EC:3.4.21.88UniRule annotation)
Gene namesi
Name:lexAUniRule annotation
Ordered Locus Names:CD630_19310
OrganismiPeptoclostridium difficile (strain 630) (Clostridium difficile)
Taxonomic identifieri272563 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium
Proteomesi
  • UP000001978 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211LexA repressorPRO_0000322724Add
BLAST

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei96 – 972Cleavage; by autolysisUniRule annotation

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272563.CD1931.

Structurei

3D structure databases

ProteinModelPortaliQ187P1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S24 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
KOiK01356.
OMAiKQHELLM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
InterProiIPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR00498. lexA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q187P1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLDLTEKQV LILEFIKSQI ILKGYPPAVR EICTAVGLRS TSTVHSHLNK
60 70 80 90 100
LEKLGYIRKD PTKPRAIEVL ERSKVNDVSG ANQEIIELPL VGQITAGEPI
110 120 130 140 150
LAQQNIEEYI PFPASLVKGS NNFVLRVKGE SMINAGILDE DYVVVDKKNT
160 170 180 190 200
ALNSQIVVAL INGESATVKR FFKEGNLIRL QPENDFMEPI MLNDSEVEIV
210
GIVTGVFRVI K
Length:211
Mass (Da):23,473
Last modified:September 21, 2011 - v2
Checksum:i8571BD9BB5103F76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ68806.2.
RefSeqiWP_009897067.1. NZ_CP010905.1.
YP_001088437.2. NC_009089.1.

Genome annotation databases

EnsemblBacteriaiCAJ68806; CAJ68806; CD630_19310.
GeneIDi4915959.
KEGGicdf:CD630_19310.
pdc:CDIF630_02135.
PATRICi19442281. VBICloDif38397_2027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ68806.2.
RefSeqiWP_009897067.1. NZ_CP010905.1.
YP_001088437.2. NC_009089.1.

3D structure databases

ProteinModelPortaliQ187P1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272563.CD1931.

Protein family/group databases

MEROPSiS24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ68806; CAJ68806; CD630_19310.
GeneIDi4915959.
KEGGicdf:CD630_19310.
pdc:CDIF630_02135.
PATRICi19442281. VBICloDif38397_2027.

Phylogenomic databases

eggNOGiENOG4105DS7. Bacteria.
COG1974. LUCA.
HOGENOMiHOG000232168.
KOiK01356.
OMAiKQHELLM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPiMF_00015. LexA. 1 hit.
InterProiIPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00726. LEXASERPTASE.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR00498. lexA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLEXA_PEPD6
AccessioniPrimary (citable) accession number: Q187P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: September 21, 2011
Last modified: September 7, 2016
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.